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Chapter 36: Transport in Plants

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Chapter 36: Transport in Plants

Transport in Plants

chapter 36 presentation ppt campbell

Resource Acquisition and Transport in Vascular Plants

chapter 36 presentation ppt campbell

Transport in Vascular Plants

chapter 36 presentation ppt campbell

TRANSPORT in PLANTS.

chapter 36 presentation ppt campbell

36.3 Transpiration drives transport of water and minerals from roots to shoots Amarisa Miles.

chapter 36 presentation ppt campbell

Chapter 36 – Plants & Transpiration. The success of plants depends on their ability to gather and conserve resources from their environment The transport.

chapter 36 presentation ppt campbell

AP Biology Chapter 36. Transport in Plants AP Biology Transport in plants  H 2 O & minerals  Sugars  Gas exchange.

chapter 36 presentation ppt campbell

Transport in Vascular Plants Chapter 36. Transport in Plants Occurs on three levels:  the uptake and loss of water and solutes by individual cells 

chapter 36 presentation ppt campbell

Question ? u How do plants move materials from one organ to the other ?

chapter 36 presentation ppt campbell

Plants Transport and Tissue Transport in plants H 2 O & minerals – transport in xylem – transpiration Sugars – transport in phloem – bulk flow.

chapter 36 presentation ppt campbell

Ch. 35 Plant Structure, Growth, and Development & Ch

chapter 36 presentation ppt campbell

Long-Distance Transport in Plants Biology 1001 November 21, 2005.

chapter 36 presentation ppt campbell

Transport in Plants.

chapter 36 presentation ppt campbell

Copyright © 2005 Pearson Education, Inc. publishing as Benjamin Cummings PowerPoint Lectures for Biology, Seventh Edition Neil Campbell and Jane Reece.

chapter 36 presentation ppt campbell

Chapter 36: Transport in Plants.

chapter 36 presentation ppt campbell

CAMPBELL BIOLOGY Reece Urry Cain Wasserman Minorsky Jackson © 2014 Pearson Education, Inc. TENTH EDITION 36 Resource Acquisition and Transport in Vascular.

chapter 36 presentation ppt campbell

Ch. 36 Warm-Up 1. Describe the process of how H 2 O gets into the plant and up to the leaves. 2. Compare and contrast apoplastic flow to symplastic flow.

chapter 36 presentation ppt campbell

NOTES: CH 36 - Transport in Plants

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LECTURE PRESENTATIONS For CAMPBELL BIOLOGY, NINTH EDITION

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chapter 36 presentation ppt campbell

Mashal Kaynat

Proteins are the building blocks of life and formed by the polypeptide chains of amino acids. Twenty amino acids are exists in nature which gives infinite variety of protein. Protein has four types of structures. Primary, secondary, tertiary and quaternary structures. Proteins are very sensitive because there are week forces among proteins due to which proteins can easily be denatured.

Tapan Dutta

Phu Tien Tran

Madi Ha Nawaz Nawaz

Proteins Protein is a polypeptide which is composed of one or more long chains of amino acids (smaller units that are nitrogenous organic compounds). Twenty different types of amino acids are used to form the protein. Protein's specific three dimensional structures and its function are determined by the specific sequence of its amino acid. These polymers of amino acids (proteins) are giant, elaborate molecules that are involved in many complex functions of the body. These are essential for the structure and function of the cell and also play important role in the guideline of tissues and organs. Proteins are used for plenty of functions, i.e. repairing and building tissues, like enzymes aiding the immune process and serving as hormones. All proteins contain the subunit the same basic sub-components beside of their differences in structure. Proteins are of the different types of macromolecules, in addition to carbohydrates, lipids (fats), & nucleic acids, such as DNA and RNA. Macromolecules are large molecules that perform specialized functions inside living organisms. The structural arrangement of a protein molecule will differ in accordance with its function. Sources: As protein play a role in tissue repair that is why it is so important to have protein in our diet. Protein can be present in all living things. The type and amount of protein within foods can vary, but inevitably it is present in meats, cheeses, poultry, seafood, and nuts beans, that tend to have higher protein content than plenty of plant-based sources. Determination of Protein structure: Primary conformation of proteins is involved in the determination of 3-D array of proteins. The protein conformation and its role in cell are determined by the amino acid sequence which is specified by the genes in cell. Protein is synthesized by the process of translation in which RNA encoded information are used for the polypeptide formation. Before this process RNA is formed by the transcription of DNA which encodes its information into RNA. The DNA has genetic information used to determine the amino acid sequence which produces the polypeptide chain of proteins. Levels of protein structure: Primary structure: Primary structure of protein Explain the initial order where amino acids are joined with each other to form any healthy proteins that are formed by twenty amino acids. Amino acids are formed by following components Alpha carbon atom bonded towards four groups beneath: • Hydrogen atom (H) • Carboxyl group (-COOH) • Amino group (-NH2) • R group which is variable Alpha carbon of the amino acids is bounded to the all these groups i.e. hydrogen, carboxyl, and amino group and " R " group differs involving amino acids as well as ascertains these variances involving most of these healthy proteins monomers. This amino acid collection of the healthy proteins relies on the data found in this cell genetic code. This is associated with amino acids inside a polypeptide exclusive as well as certain to a particular healthy protein. Changing 1 amino acid position can cause any gene mutation; this generally ends in any non-functioning healthy proteins. Secondary structure: This is involved in describing twist of the polypeptide that provides the three dimension array of protein. There are 2 sorts of second set ups affecting the protein. First form could be the alpha helix and this specific construction is similar to a folded spring which is collateralized simply through hydrogen connecting inside the polypeptide. The second construction throughout proteins could be the beta pleated sheet. This specific construction seems to be already

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Campbell chapter outlines

chapter 36 presentation ppt campbell

CAMPBELL CHAPTER OUTLINES Chapter outlines

  • Chapter 01 – Exploring Life
  • Chapter 02 – The Chemical Context of Life
  • Chapter 03 – Water and the Fitness of the Environment
  • Chapter 04 – Carbon and the Molecular Diversity of Life
  • Chapter 05 – The Structure and Function of Macromolecules
  • Chapter 06 – A Tour of the Cell
  • Chapter 07 – Membrane Structure and Function
  • Chapter 08 – An Introduction to Metabolism
  • Chapter 09 – Cellular Respiration: Harvesting Chemical Energy
  • Chapter 33 – Invertebrates
  • Chapter 34 – Vertebrates
  • Chapter 35 – Plant Structure
  • Chapter 10 – Photosynthesis
  • Chapter 11 – Cell Communication
  • Chapter 12 – The Cell Cycle
  • Chapter 13 – Meiosis and Sexual Life Cycles
  • Chapter 14 – Mendel and the Gene Idea
  • Chapter 15 – The Chromosomal Basis of Inheritance
  • Chapter 16 – The Molecular Basis of Inheritance
  • Chapter 17 – From Gene to Protein
  • Chapter 18 – The Genetics of Viruses and Bacteria
  • Chapter 19 – Eukaryotic Genomes
  • Chapter 20 – DNA Technology and Genomics
  • Chapter 21 – The Genetic Basis of Development
  • Chapter 22 – Descent with Modification: Darwinian View of Life
  • Chapter 23 – The Evolution of Populations
  • Chapter 24 – The Origin of Species
  • Chapter 25 – Phylogeny and Systematics
  • Chapter 26 – The Tree of Life: An Introduction to Biological Diversity
  • Chapter 27 – Prokaryotes
  • Chapter 28 – Protists
  • Chapter 29 – Plant Diversity I: How Plants Colonized Land
  • Chapter 30 – Plant Diversity II: The Evolution of Seed Plants
  • Chapter 31 – Fungi
  • Chapter 32 – An Introduction to Animal Diversity
  • Chapter 36 – Transport in Vascular Plants
  • Chapter 37 – Plant Nutrition
  • Chapter 38 – Angiosperm Reproduction and Biotechnology
  • Chapter 39 – Plant Responses to Internal and External Signals
  • Chapter 40 – Basic Principles of Animal Form and Function
  • Chapter 41 – Animal Nutrition
  • Chapter 42 – Circulation and Gas Exchange
  • Chapter 43 – The Immune System
  • Chapter 44 – Osmoregulation and Excretion
  • Chapter 45 – Hormones and the Endocrine System
  • Chapter 46 – Animal Reproduction
  • Chapter 47 – Animal Development
  • Chapter 48 – Nervous Systems
  • Chapter 50 – An Introduction to Ecology and the Biosphere
  • Chapter 51 – Behavioral Ecology
  • Chapter 52 – Population Ecology
  • Chapter 53 – Community Ecology
  • Chapter 54 – Ecosystems
  • Chapter 55 – Conservation Biology and Restoration Ecology
  • Campbell’s Biology, 6th Edition
  • Campbell’s Biology, 7th Edition
  • Campbell’s Biology, 8th Edition
  • 01 – Science of Biology
  • 02 – Nature of Molecules
  • 03 – Chemical Building Blocks of Life
  • 04 – Origin/Early History of Life
  • 05 – Cell Structure
  • 06 – Membranes
  • 07 – Cell-Cell Interactions
  • 08 – Energy and Metabolism
  • 09 – Cellular Respiration
  • 10 – Photosynthesis
  • 11 – Cell Division
  • 12 – Meiosis
  • 13 – Patterns of Inheritance
  • 14 – DNA: Genetic Material
  • 15 – How Genes Work
  • 16 – Gene Technology
  • 17 – Genomes
  • 18 – Control of Gene Expression
  • 19 – Cellular Mechanisms of Development
  • 20 – Nervous System
  • 21 – Sensory Systems
  • 22 – Endocrine System
  • 23 – Sex/Reproduction
  • 24 – Circulatory/Respiratory Systems
  • 25 – Immune System
  • 26 – Renal System, Digestive System
  • 27 – Protists, Fungi
  • 28 – Evolution of Plants
  • 29 – Plant Body
  • 30 – Plant Reproduction
  • 31 – Plant Development
  • 32 – Evolution
  • 33 – Behavioral Ecology
  • 34 – Community Ecology

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chapter 36 presentation ppt campbell

A Tour of the Cell

LECTURE PRESENTATIONS

For CAMPBELL BIOLOGY, NINTH EDITION

Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson

© 2011 Pearson Education, Inc.

Lectures by

Erin Barley

Kathleen Fitzpatrick

Overview: The Fundamental Units of Life

  • All organisms are made of cells
  • The cell is the simplest collection of matter �that can be alive
  • Cell structure is correlated to cellular function
  • All cells are related by their descent from earlier cells

Figure 6.1 How do your brain cells help you learn about biology?

Brightfield

(unstained specimen)

(stained specimen)

Differential-interference-�contrast (Nomarski)

Fluorescence

Deconvolution

Super-resolution

Scanning electron�microscopy (SEM)

Transmission electron�microscopy (TEM)

Cross section�of cilium

Longitudinal section�of cilium

Electron Microscopy (EM)

Light Microscopy (LM)

Phase-contrast

Comparing Prokaryotic and Eukaryotic Cells

  • Basic features of all cells

Plasma membrane

  • Semifluid substance called cytosol
  • Chromosomes (carry genes)
  • Ribosomes (make proteins)
  • Prokaryotic cells – Archae and Bacteria
  • DNA in an unbound region called the nucleoid
  • No membrane-bound organelles
  • Cytoplasm bound by the plasma membrane
  • Eukaryotic cells
  • DNA in a nucleus that is bounded by a membranous nuclear envelope
  • Membrane-bound organelles
  • Cytoplasm in the region between the plasma membrane and nucleus
  • Larger than prokaryotes

Figure 6.5 A prokaryotic cell.

Bacterial�chromosome

A typical�rod-shaped�bacterium

Plasma�membrane

A thin section�through the�bacterium Bacillus�coagulans (TEM)�

  • The plasma membrane - a selective barrier that allows sufficient passage of oxygen, nutrients, and waste to service the volume of every cell
  • The general structure of a biological membrane is a double layer of phospholipids
  • 30-300 μm circumference

Outside of cell

Inside of cell

TEM of a plasma�membrane

Hydrophilic�region

Hydrophobic�region

Carbohydrate side chains

Phospholipid

(b) Structure of the plasma membrane

Surface area increases while�total volume remains constant

Total surface area�[sum of the surface areas�(height × width) of all box�sides × number of boxes]

Total volume�[height × width × length�× number of boxes]

Surface-to-volume�(S-to-V) ratio�[surface area ÷ volume]

A Panoramic View of the Eukaryotic Cell

  • A eukaryotic cell has internal membranes that partition the cell into organelles
  • Plant and animal cells have most of the same organelles

Figure 6.8a

ENDOPLASMIC RETICULUM (ER)

Nuclear�envelope

  • Golgi apparatus

Mitochondrion

Microtubules

  • Intermediate filaments
  • Microfilaments

CYTOSKELETON:

Figure 6.8b

Animal Cells

Human cells from lining�of uterus (colorized TEM)

Yeast cells budding�(colorized SEM)

Fungal Cells

Parent�cell

A single yeast cell�(colorized TEM)

Figure 6.8c

Golgi�apparatus

Wall of adjacent cell

Plasmodesmata

Chloroplast

Intermediate�filaments

CYTOSKELETON

Central vacuole

Smooth�endoplasmic�reticulum

Rough�endoplasmic�reticulum

Figure 6.8d

Plant Cells

Cells from duckweed�(colorized TEM)

Protistan Cells

Chlamydomonas� (colorized SEM)

Chlamydomonas� (colorized TEM)

Concept 6.3: Nucleus, DNA, and Ribosomes

  • The nucleus contains most of the DNA in a eukaryotic cell
  • Ribosomes use the information from the DNA to make proteins

The Nucleus: Information Central

  • Nucleus - contains most of the cell’s genes and is the most conspicuous organelle
  • nuclear envelope - encloses the nucleus, separating it from the cytoplasm

A double membrane; each membrane consists of a lipid bilayer

Figure 6.9a

Nuclear envelope:

Inner membrane

Outer membrane

Nuclear pore

Pore�complex

Close-up�of nuclear�envelope

Figure 6.9b

Surface of nuclear�envelope

Figure 6.9c

Pore complexes (TEM)

Nuclear lamina (TEM)

Pores- regulate the entry and exit of molecules from the nucleus

The shape of the nucleus is maintained by the nuclear lamina , which is composed of protein

  • In the nucleus, DNA is organized into discrete units called chromosomes
  • Each chromosome is composed of a single DNA molecule associated with proteins
  • The DNA and proteins of chromosomes are together called chromatin
  • Chromatin condenses to form discrete chromosomes as a cell prepares to divide
  • The nucleolus is located within the nucleus and is the site of ribosomal RNA (rRNA) synthesis
  • Ribosomes are particles made of ribosomal RNA and protein
  • Ribosomes carry out protein synthesis in two locations
  • In the cytosol (free ribosomes)
  • On the outside of the endoplasmic reticulum or the nuclear envelope (bound ribosomes)

Figure 6.10

Ribosomes bound to ER

Ribosomes: Protein Factories

Concept 6.4: The endomembrane system - regulates protein traffic and performs metabolic functions in the cell

  • Components of the endomembrane system
  • Nuclear envelope
  • Endoplasmic reticulum
  • These components are either continuous or connected via transfer by vesicles

The Endoplasmic Reticulum: Biosynthetic Factory

  • The endoplasmic reticulum (ER) accounts for more than half of the total membrane in many eukaryotic cells
  • The ER membrane is continuous with the nuclear envelope
  • There are two distinct regions of ER
  • Smooth ER , which lacks ribosomes
  • Rough ER , surface is studded with ribosomes

Figure 6.11a

Transport vesicle

Transitional ER

Figure 6.11b

Functions of the ER

  • The rough ER
  • Has bound ribosomes, which secrete glycoproteins (proteins covalently bonded to carbohydrates)
  • Distributes transport vesicles, proteins surrounded by membranes
  • Is a membrane factory for the cell
  • The smooth ER
  • Synthesizes lipids – sex cells and adrenal glands
  • Metabolizes carbohydrates
  • Detoxifies drugs and poisons- liver cells
  • Stores calcium ions - muscles

The Golgi Apparatus: Shipping and �Receiving Center

  • The Golgi apparatus consists of flattened membranous sacs called cisternae
  • Functions of the Golgi apparatus
  • Modifies products of the ER – glycoproteins and phospholipids
  • Manufactures certain macromolecules – pectin
  • Sorts and packages materials into transport vesicles –molecular tagging for docking sites

Figure 6.12

cis face�(“receiving” side of�Golgi apparatus)�

trans face�(“shipping” side of�Golgi apparatus)

TEM of Golgi apparatus

Lysosomes: Digestive Compartments

  • A lysosome is a membranous sac of hydrolytic enzymes that can digest macromolecules
  • Lysosomal enzymes can hydrolyze proteins, fats, polysaccharides, and nucleic acids
  • Lysosomal enzymes work best in the acidic environment inside the lysosome
  • Some types of cell (amoeba and white blood cells) can engulf another cell by phagocytosis ; this forms a food vacuole
  • fuses with the food vacuole and digests the molecules
  • use enzymes to recycle the cell’s own organelles and macromolecules, a process called autophagy

Figure 6.13

Digestive�enzymes

Food vacuole

(a) Phagocytosis

Vesicle containing�two damaged�organelles

Mitochondrion�fragment

Peroxisome�fragment

(b) Autophagy

Figure 6.13b

Vacuoles: Diverse Maintenance Compartments

  • A plant cell or fungal cell may have one or several vacuoles , derived from endoplasmic reticulum and Golgi apparatus
  • Food vacuoles are formed by phagocytosis
  • Contractile vacuoles , found in many freshwater protists, pump excess water out of cells
  • Central vacuoles , found in many mature plant cells, hold organic compounds and water

Figure 6.14

Central�vacuole

Figure 6.15-1

Figure 6.15-2

trans Golgi

Figure 6.15-3

Concept 6.5: Mitochondria and chloroplasts change energy from one form to another

  • Mitochondria are the sites of cellular respiration, a metabolic process that uses oxygen to generate ATP
  • Chloroplasts , found in plants and algae, are the sites of photosynthesis
  • Peroxisomes are oxidative organelles

The Evolutionary Origins of Mitochondria and Chloroplasts

  • Mitochondria and chloroplasts have similarities with bacteria
  • Enveloped by a double membrane
  • Contain free ribosomes and circular DNA molecules
  • Grow and reproduce somewhat independently in cells
  • The Endosymbiont theory
  • An early ancestor of eukaryotic cells engulfed a nonphotosynthetic prokaryotic cell, which formed an endosymbiont relationship with its host
  • The host cell and endosymbiont merged into a single organism, a eukaryotic cell with a mitochondrion
  • At least one of these cells may have taken up a photosynthetic prokaryote, becoming the ancestor of cells that contain chloroplasts

Figure 6.16

Endoplasmic�reticulum

Nuclear �envelope

Ancestor of�eukaryotic cells�(host cell)

Engulfing of oxygen-�using nonphotosynthetic�prokaryote, which�becomes a mitochondrion

Nonphotosynthetic�eukaryote

At least�one cell

Photosynthetic eukaryote

Engulfing of�photosynthetic�prokaryote

Mitochondria: Chemical Energy Conversion

  • Found in eukaryotes
  • smooth outer membrane and an inner membrane folded into cristae
  • The inner membrane creates two compartments: intermembrane space and mitochondrial matrix
  • Some metabolic steps of cellular respiration are catalyzed in the mitochondrial matrix
  • Cristae present a large surface area for enzymes that synthesize ATP

Figure 6.17

Intermembrane space

Free�ribosomes�in the�mitochondrial�matrix

(a) Diagram and TEM of mitochondrion

Network of mitochondria in a protist�cell (LM)

Mitochondrial�DNA

Nuclear DNA

Mitochondria

Chloroplasts: Capture of Light Energy

  • Chloroplast structure includes
  • Thylakoids , membranous sacs, stacked to form a granum
  • Stroma , the internal fluid
  • The chloroplast is one of a group of plant organelles, called plastids
  • contain the green pigment chlorophyll
  • contains enzymes and other molecules that function in photosynthesis
  • found in leaves and other green organs of plants and in algae

Figure 6.18

Inner and outer

(a) Diagram and TEM of chloroplast

(b) Chloroplasts in an algal cell

Chloroplasts�(red)

Peroxisomes: Oxidation

  • specialized metabolic compartments bounded by a single membrane
  • Remove H+ to O+ which produces hydrogen peroxide and convert it to water
  • Glyoxysomes – found in plant seed and fatty acids to sugar for the cotyledon until photosynthesis begins

Figure 6.19

Concept 6.6: The cytoskeleton is a network of fibers that organizes structures and activities in the cell

  • Extends throughout the cytoplasm
  • Organizes the cell’s structures and activities, anchoring many organelles
  • Composed of three types of molecular structures
  • Support the cell and maintain its shape
  • It interacts with motor proteins to produce motility (flagella/cilia;muscle contraction; plasma membrane; cytostreaming
  • Inside the cell, vesicles can travel along “monorails” provided by the cytoskeleton

Figure 6.20

Figure 6.21

Motor protein�(ATP powered)

Microtubule�of cytoskeleton

Receptor for�motor protein

Microtubule

Components of the Cytoskeleton

  • Microtubules – thickest; organelle movement; secretory vesicles to plasma membrane; mitosis
  • Microfilaments – thinnest (also called actin ) –supports cell shape; microvilli; forms bridge with myosin for muscle contraction;cell contraction during cell cleavage; pseudopodia movement (amoeba and WBC)
  • Intermediate filaments -diameters in a middle range – contains protein keratin; reinforces position of nucleus;nuclear lamina; axons

Column of tubulin dimers

Tubulin dimer

Actin subunit

Keratin proteins

Fibrous subunit (keratins�coiled together)

Centrosomes and Centrioles

  • centrosome near the nucleus; microtubules grow from it
  • In animal cells , the centrosome has a pair of centrioles , each with nine triplets of microtubules arranged in a ring

Figure 6.22

Longitudinal�section of�one centriole

Cross section�of the other centriole

Cilia and Flagella

  • Microtubules control the beating of cilia and flagella , locomotor appendages of some cells
  • Cilia and flagella differ in their beating patterns
  • Cilia and flagella share a common structure
  • A core of microtubules sheathed by the plasma membrane
  • A basal body that anchors the cilium or flagellum
  • A motor protein called dynein , which drives the bending movements of a cilium or flagellum

Figure 6.23

Direction of swimming

(b) Motion of cilia

Direction of organism’s movement

Power stroke Recovery stroke

(a) Motion of flagella

Figure 6.24

Longitudinal section�of motile cilium

Cross section of�motile cilium

Outer microtubule�doublet

Dynein proteins

Central�microtubule

Radial�spoke

Cross-linking�proteins between�outer doublets

Cross section of�basal body

  • How dynein “walking” moves flagella and cilia
  • Dynein arms alternately grab, move, and release the outer microtubules
  • Protein cross-links limit sliding
  • Forces exerted by dynein arms cause doublets to curve, bending the cilium or flagellum

Figure 6.25a

Microtubule�doublets

Dynein protein

(a) Effect of unrestrained dynein movement

Figure 6.25b

Cross-linking proteins�between outer doublets

Anchorage�in cell

(b) Effect of cross-linking proteins

(c) Wavelike motion

Figure 6.27

Muscle cell

(a) Myosin motors in muscle cell contraction

Cortex (outer cytoplasm):�gel with actin network

Inner cytoplasm: sol�with actin subunits

(b) Amoeboid movement

Extending�pseudopodium

(c) Cytoplasmic streaming in plant cells

  • Cytoplasmic streaming is a circular flow of cytoplasm within cells
  • This streaming speeds distribution of materials within the cell
  • In plant cells, actin-myosin interactions and sol-gel transformations drive cytoplasmic streaming

Concept 6.7: Extracellular components and connections between cells help coordinate cellular activities

  • Most cells synthesize and secrete materials that are external to the plasma membrane
  • These extracellular structures include
  • Cell walls of plants
  • The extracellular matrix (ECM) of animal cells
  • Intercellular junctions

Cell Walls of Plants

  • An extracellular structure that distinguishes plant cells from animal cells
  • Prokaryotes, fungi, and some protists also have cell walls
  • The cell wall protects the plant cell, maintains its shape, and prevents excessive uptake of water
  • Plant cell walls are made of cellulose fibers embedded in other polysaccharides and protein
  • Plant cell walls may have multiple layers
  • Primary cell wall : relatively thin and flexible
  • Middle lamella : thin layer between primary walls of adjacent cells
  • Secondary cell wall (in some cells): added between the plasma membrane and the primary cell wall

Figure 6.28

Secondary�cell wall

Primary�cell wall

Middle�lamella

Plant cell walls

Figure 6.29

Distribution of cellulose�synthase over time

Distribution of�microtubules�over time

The Extracellular Matrix (ECM) of Animal Cells

  • Animal cells lack cell walls but are covered by an elaborate extracellular matrix (ECM)
  • The ECM is made up of glycoproteins such as collagen , proteoglycans , and fibronectin
  • ECM proteins bind to receptor proteins in the plasma membrane called integrins
  • Functions of the ECM

Figure 6.30

EXTRACELLULAR FLUID

Fibronectin

Proteoglycan�complex

Polysaccharide�molecule

Carbo-�hydrates

Proteoglycan�molecule

Proteoglycan complex

Cell Junctions

  • Neighboring cells in tissues, organs, or organ systems often adhere, interact, and communicate through direct physical contact

Plasmodesmata in Plant Cells

  • Plasmodesmata are channels that perforate plant cell walls
  • Through plasmodesmata, water and small solutes (and sometimes proteins and RNA) can pass from cell to cell

Figure 6.31

Interior�of cell

Plasma membranes

Tight Junctions, Desmosomes, and Gap Junctions in Animal Cells

  • At tight junctions , membranes of neighboring cells are pressed together, preventing leakage of extracellular fluid (skin cells)
  • Desmosomes (anchoring junctions) fasten cells together into strong sheets (muscle cells to muscle cells)
  • Gap junctions (communicating junctions) provide cytoplasmic channels between adjacent cells – (heart)

Figure 6.32a

Tight junctions prevent�fluid from moving�across a layer of cells

Extracellular�matrix

Plasma membranes�of adjacent cells

Space�between cells

Ions or small�molecules

Tight junction

Gap�junction

Figure 6.32b

Figure 6.33

intro to metabolism campbell chapter 6

Intro to Metabolism Campbell Chapter 6

Jan 04, 2020

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Intro to Metabolism Campbell Chapter 6. http://www.gifs.net. http://ag.ansc.purdue.edu/sheep/ansc442/Semprojs/2003/spiderlamb/eatsheep.gif. Metabolism is the sum of an organism’s chemical reactions

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  • activation energy
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  • enzymes lower activation energy

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Presentation Transcript

Intro to MetabolismCampbell Chapter 6 http://www.gifs.net http://ag.ansc.purdue.edu/sheep/ansc442/Semprojs/2003/spiderlamb/eatsheep.gif

Metabolism is the sum of an organism’s chemical reactions • Metabolism is an emergent property of life that arises from interactions between molecules within the cell http://www.encognitive.com/images/metabolic-pathways.png

A metabolic pathway begins with a specific molecule and ends with a product • Each step is catalyzed by a specific enzyme BIOCHEMICAL PATHWAYVIDEO

ENZYMES THAT WORK TOGETHER IN A PATHWAY CAN BE Concentrated in specific location Covalently bound incomplex Soluble with free floating intermediates Attached toa membranein sequence Biochemistry Lehninger

CATABOLIC PATHWAY (CATABOLISM)Release of energy by the breakdown of complex molecules to simpler compoundsEX: digestive enzymes break down food ANABOLIC PATHWAY (ANABOLISM)consumes energy to build complicated molecules from simpler onesEX: linking amino acids to form proteins http://www.sciencelearn.org.nz/var/sciencelearn/storage/images/contexts/nanoscience/sci_media/images/chemical_reactions_involve_making_new_combinations/53823-2-eng-NZ/chemical_reactions_involve_making_new_combinations_full_size_landscape.jpg

Krebs Cycle connects the catabolic and anabolic pathways http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/I/IntermediaryMetabolism.html

Forms of Energy • ENERGY = capacity to cause change • Energy exists in various forms (some of which can perform work) • Energy can be converted from one form to another

KINETICENERGY – energy associated with motion • HEAT (thermal energy) is kinetic energy associated with random movement of atoms or molecules POTENTIALENERGY = energy that matter possesses because of its location or structure • CHEMICAL energy is potential energy available for release in a chemical reaction

Diving converts potential energy to kinetic energy. On the platform, the diver has more potential energy. In the water, the diver hasless potential energy. Climbing up converts kinetic energy of muscle movement to potential energy.

THERMODYNAMICS = the study of energy transformations • CLOSED system (EX: liquid in a thermos) = isolated from its surroundings • OPEN system energy + matter can be transferred between the system and its surroundings • Organisms are open systems http://ag.ansc.purdue.edu/sheep/ansc442/Semprojs/2003/spiderlamb/eatsheep.gif

The First Law of Thermodynamics = energy of the universe is constant • Energy can be transferred and transformed • Energy cannot be created or destroyed • The first law is also called the principle of CONSERVATION OF ENERGY http://www.pxleyes.com/photoshop-picture/4a3b747566555/remote-control.htmlhttp://www.suncowboy.com/solar101.php

The Second Law of Thermodynamics During every energy transfer or transformation • entropy (disorder) of the universe INCREASES • some energy is unusable, often lost as heat http://hyperphysics.phy-astr.gsu.edu/hbase/therm/entrop.html http://www.janebluestein.com/articles/whatswrong.html

Second law of thermodynamics First law of thermodynamics Chemical energy Heat CO2 H2O ORGANISMS are energy TRANSFORMERS! Spontaneous processes occur without energy input; they can happen quickly or slowly For a process to occur without energy input, it must increase the entropy of the universe

Free-Energy Change (G) can help tell which reactions will happen ∆G = change in free energy ∆H = change in total energy (enthalpy) or change ∆S = entropy T = temperature ∆G = ∆H - T∆S • Only processes with a negative ∆G are spontaneous • Spontaneous processes can be harnessed to perform work

Exergonic and Endergonic Reactions in Metabolism • EXERGONIC reactions (- ∆G) • Release energy • are spontaneous ENDERGONIC reactions (+ ∆G) • Absorb energy fromtheir surroundings • are non-spontaneous

Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions • A cell does three main kinds of work: • Mechanical • Transport • Chemical • In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction • Overall, the coupled reactions are exergonic

ATP (adenosine triphosphate) is the cell’s renewable and reusable energy shuttle ATP provides energy for cellular functions Energy to charge ATP comes from catabolic reactions Adenine Phosphate groups Ribose

LE 8-9 P P P Adenosine triphosphate (ATP) H2O + P P P + Energy i Adenosine diphosphate (ADP) Inorganic phosphate

ATP Energy for cellular work provided by the loss ofphosphate from ATP Energy from catabolism (used to charge upADP into ATP ADP + P i

Endergonic reaction: DG is positive, reaction is not spontaneous NH2 NH3 DG = +3.4 kcal/mol + Glu Glu Ammonia Glutamine Glutamic acid Exergonic reaction: DG is negative, reaction is spontaneous P ATP ADP DG = –7.3 kcal/mol H2O + + i Coupled reactions: Overall DG is negative; Together, reactions are spontaneous DG = –3.9 kcal/mol

LE 8-11 P i P Protein moved Motor protein Mechanical work: ATP phosphorylates motor proteins Membrane protein ADP ATP + P i P P i Solute transported Solute Transport work: ATP phosphorylates transport proteins P NH2 NH3 P + + Glu i Glu Reactants: Glutamic acid and ammonia Product (glutamine) made Chemical work: ATP phosphorylates key reactants

Every chemical reaction between molecules involves bond breaking and bond forming ACTIVATION ENERGY = amount of energy required to get chemical reaction started Activation energy is often supplied in the form of heat from the surroundings Free energy animation IT’S LIKE PUSHING A SNOWBALL UP A HILL . . . Once you get it up there, it can roll down by itself http://www.chuckwagondiner.com/art/matches.jpg http://plato.acadiau.ca/COURSES/comm/g5/Fire_Animation.gif

The Activation Energy Barrier LE 8-14 B A C D Transition state EA B A Free energy D C Reactants B A DG < O C D Products Progress of the reaction

CATALYST = a chemical agent that speeds up a reaction without being consumed by the reaction ENZYMES = biological catalystsMost enzymes are PROTEINS Exception = ribozymes (RNA) Ch 17 & 26

Course of reaction without enzyme EA without enzyme EA with enzyme is lower Reactants Free energy Course of reaction with enzyme DG is unaffected by enzyme Products Progress of the reaction ENZYMES work by LOWERING ACTIVATION ENERGY;

ENZYMES LOWER ACTIVATION ENERGY BY • Orienting substrates correctly • Straining substrate bonds • Providing a favorable microenvironment Enzymes change ACTIVATION ENERGY but NOT energy of REACTANTS or PRODUCTS http://sarahssureshots.wikispaces.com/Focus+on+Proteins http://www.ac-montpellier.fr/sections/personnelsen/ressources-pedagogiques/education-artistique/consultation-avis-du

ENZYMES • Most are proteins • Lower activation energy • Specific • Shape determines function • Reusuable • Unchanged by reaction Image from: http://www.hillstrath.on.ca/moffatt/bio3a/digestive/enzanim.htm

The REACTANT that an enzyme acts on = SUBSTRATE • Enzyme + substrate =ENZYME-SUBSTRATE COMPLEX • Region on the enzyme where the substrate binds = ACTIVE SITE • Substrate held in active site by WEAK interactions (ie. hydrogen and ionic bonds)

TWO MODELS PROPOSED • LOCK & KEYActive site on enzymefits substrate exactly • INDUCED FITBinding of substrate causes changein active site so it fits substratemore closely http://www.grand-illusions.com/images/articles/toyshop/trick_lock/mainimage.jpg http://commons.wikimedia.org/wiki/File:Induced_fit_diagram.png

Enzyme Activity can be affected by: • General environmental factors, such as temperature, pH, salt concentration, etc. • Chemicals that specifically influence the enzyme See a movie Choose narrated http://www.desktopfotos.de/Downloads/melt_cd.jpg http://www.nealbrownstudio.com/adm/photo/163_nb_fried_egg.jpg

TEMPERATURE & ENZYME ACTIVITY Each enzyme has an optimal temperature at which it can function (Usually near body temp) http://www.animated-gifs.eu/meteo-thermometers/001.htm

http://www.uic.edu/classes/bios/bios100/lectures/chemistry.htm http://www.uic.edu/classes/bios/bios100/lectures/chemistry.htm Increasing temperature increases the rate of an enzyme-catalyzed reaction up to a point. Above a certain temperature, activity begins to decline because the enzyme begins to denature.

pH and ENZYME ACTIVITYEach enzyme has an optimal pH at which it can function

http://www.wissensdrang.com/media/wis9r.gif COFACTORS= non-protein enzyme helpers • EX: Zinc, iron, copper COENZYMES= organic enzyme helpers • Ex: vitamins http://www.elmhurst.edu/~chm/vchembook/595FADcoq.html

SUBSTRATE CONCENTRATION & ENZYME ACTIVITY ← V MAX Adding substrate increases activity up to a point

REGULATION OF ENZYME PATHWAYS • GENE REGULATIONcell switches on or off the genes that code for specific enzymes

REGULATION OF ENZYME PATHWAYS • FEEDBACK INHIBITIONend product of a pathway interacts with and “turns off” an enzyme earlier in pathway • prevents a cell from wasting chemical resources by synthesizing more product than is needed FEEDBACK INHIBITION

A A Negative feedback Enzyme 1 Enzyme 1 B B Enzyme 2 C C Enzyme 3 D D D D D D D D D D D NEGATIVE FEEDBACK • An accumulation of an end product slows the process that produces that product Example: sugar breakdown generates ATP; excess ATP inhibits an enzyme near the beginning of the pathway

W W Enzyme 4 Enzyme 4 Positivefeedback X X Enzyme 5 Enzyme 5 Y Y Enzyme 6 Enzyme 6 Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z Z POSITIVE FEEDBACK (less common) • The end product speeds up production EXAMPLE: Chemicals released by platelets that accumulate at injury site, attract MORE platelets to the site.

REGULATION OF ENZYME ACTIVITY • ALLOSTERIC REGULATIONprotein’s function at one site is affected by binding of a regulatory molecule at another site • Allosteric regulation can inhibit or stimulate an enzyme’s activity Allosteric enzyme inhibition http://bio.winona.edu/berg/ANIMTNS/allostan.gif

SOME ALLOSTERIC ENZYMES HAVE MULTIPLE SUBUNITS • Each enzyme has active and inactive forms • The binding of an ACTIVATOR stabilizes the active form • The binding of an INHIBITOR stabilizes the inactive form

Binding of one substrate molecule to active site of one subunit locks all subunits in active conformation. Substrate Inactive form Stabilized active form Cooperativity another type of allosteric activation

COOPERATIVITY= form of allosteric regulation that can amplify enzyme activity Binding of one substrate to active site of one subunit locks all subunits in active conformation

Enzyme Inhibitors COMPETITIVE inhibitor REVERSIBLE; Mimics substrate and competes with substrate for active site on enzyme ENZYMEANIMATION

Enzyme Inhibitors NONCOMPETITIVE inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective ENZYMEANIMATION

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