Chapter 5~ The Structure & Function of Macromolecules 5.1-5.5.
CHAPTER 5 The Structure and Function of Macromolecules.
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Transcript of CHAPTER 5 The Structure and Function of Macromolecules.
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CHAPTER 5
The Structure and Function of
Macromolecules
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KEY CONCEPTS
Focus on how STRUCTURE and biochemical properties relate to FUNCTION
Focus on how building block MONOMERS are bonded together by specific LINKAGES
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KEY CONCEPTS
Common SYNTHESIS and
BREAKDOWN reactions
Macromolecules are POLYMERS• MER - units TRI - three• POLY - many DI - two• OLIGO - several MONO - one
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POLYMERSmonomer + monomer + monomer +
monomer = a big ‘ol polymer
Unity within diversity the same monomers are common to all
forms of life
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How to make a Macromolecule
DEHYDRATION SYNTHESIS - bonding of small subunits to form a larger end product by removing water.
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Figure 5.2 The synthesis and breakdown of polymers
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How to breakdown a macromolecule…
HYDROLYSIS - digestion or degradation of large polymers by the addition of water
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Main Classes Of Macromolecules
CARBOHYDRATES LIPIDS PROTEINS NUCLEIC ACIDS
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Carbohydrates Sugars end in -ose aldehydes & ketones Isomer City General formula:
•C H2 O
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CARBOHYDRATES MONOSACCHARIDES
examples:•glucose C6 hexose•ribose C5 pentose•glyceraldehyde C3 triose
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Identify the carbons
Linear vs. ring structure ?????
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DISACCHARIDES
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DISACCHARIDES Monosaccharide monomers
Dehydration synthesis
Glycosidic linkages• 1-4 glycosidic linkage (maltose)• 1-2 glycosidic linkage (sucrose)
BIOFUNCTION: transport of fuel
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CARBOHYDRATES
POLYSACCHARIDES (100’S --> 1000’S)
StorageSTARCH (plants)
1-4 linkage, unbranched helixGLYCOGEN (animals)
1-6 linkage, branching helix
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Figure 5.6 Storage polysaccharides
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Molecular Shape
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CARBOHYDRATES MORE POLYSACCHARIDES
StructuralCELLULOSE - plant cell walls
– most abundant organic molecule – linear fibrils -> rope --> composite– alpha vs. beta glucose/digestion
CHITIN - exoskeletons & cell walls- tough, insoluble
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Figure 5.9 Chitin, a structural polysaccharide: exoskeleton and surgical thread
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Figure 5.8 The arrangement of cellulose in plant cell walls
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CARBOHYDRATES
Summary of biofunctions
Immediate fuel
Storage & transport of fuel
Structural building material
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LipidsA diverse group,
Insoluble in water,hydrophobic,
nonpolar, mostly hydrocarbon chains
technically not polymers??
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LIPIDS Fats or Triglycerides
•glycerol + 3 fatty acids
•R -COOH hydrocarbon chain 14-18 carbons + carboxyl group
•ester linkage
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LIPIDS
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LIPIDSSATURATED
• fully saturated w/ hydrogens• animal fats - solid at room temp.
UNSATURATED • at least one double bond (kink)• plant oils -liquid at room temp.• geometric isomers (cis & trans)
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Figure 5.11 Examples of saturated and unsaturated fats and fatty acids
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MORE LIPIDS PHOSPHOLIPIDS
• glycerol + 2 fatty acids + phosphate + charged group
• hydrophilic head• hydrophobic tail
BIOFUNCTION: membranes & micelles
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MORE LIPIDS STEROIDS
•4 rings + fat tail •3 cyclohexanes + cyclopentane
+ hydrocarbon chain
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MORE LIPIDS STEROIDS
•CHOLESTEROL is modified to form steroid hormones –sex hormones + corticoids
•CHOLESTEROL is also found in cell membranes
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CHOLESTEROL
One of the most misunderstood chemicals in the human body
Cho gets a BAD reputation for Atherosclerosis Coronary Heart Disease Heart Attacks Strokes High Blood Pressure
but….
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The Facts About Cholesterol
Precursor for steroid hormones Precursor for bile acids Necessary component of cell
membranes
Poor diet and hereditary factors predispose individuals to heart disease
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Proteins “first place”
over 50% dry weight of most cells
structure fits function
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Proteins Fiberous Enzymes Membrane
Channels Cell
Recognition Hormones
Transport Contraction Defense Osmotic
Homeostasis Gene
Regulators
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Check out the animations online
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Figure 5.1 Building models to study the structure and function of macromolecules
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PROTEINS Building block monomers
are amino acids basic amino acid
structure 20 different R groups
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Protein:
High-molecular weight, nitrogen-containing organic compound.
Composed of one or more polypeptides.
Polypeptides are composed of amino acids.
Amino Acid:
Contains the following bonded to a central carbon atom.
Amino groups (NH2)
Carboxyl group (COOH)
Hydrogen atom
R group (different in each amino acid)
Typically charged in the cell (-NH3
+ and COO-)
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Fig. 6.1
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Fig. 6.2. Acidic and basic amino acids.
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Figure 5.15 The 20 amino acids of proteins: nonpolar
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Fig. 6.2. Neutral, non-polar (hydrophobic) amino acids.
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Fig. 6.2. Neutral, polar (hydrophilic) amino acids.
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Amino acids are joined to form unbranched polypeptides by a peptide bond.
Peptide bond = covalent bond between the carboxyl group of one amino acid and amino group of the next amino acid.
N-terminus C-terminus
5’ (DNA) 3’ (DNA)
Fig. 6.3
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Amino Acid SummarySide Groups Determine Chemical
Properties
Nonpolar C-H tend to hydrophobic aggregate toward center
Polar O-H, N-H are hydrophilic & tend to be found on the outside
Charged acidic (-COOH) fold to outsidebasic (-NH3) fold to outside
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PROTEINS Peptide bond formation
Amino group + carboxylic acid via dehydration synthesis
Residues
N-terminus - polypeptide chain -C-terminus
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PRIMARY STRUCTURE • sequence of
AA’s• genetically
determined• involves
peptide bonds
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PRIMARY STRUCTURE
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Figure 5.20 The secondary structure of a protein
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TERTIARY STRUCTURE
• interactions between R groups
• hydrophobic interactions
• ionic bonds
• H-bonds
• disulfide bridges between cysteine
residues
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Figure 5.22 Examples of interactions contributing to the tertiary structure of a protein
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QUATERNARY STRUCTURE
• two or more polypeptide
chains needed to form one
functional protein
• Insulin - 2 AA chains
• Collagen - 3 AA chains
• Hemoglobin - 4 AA chains
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Proteins show four hierarchical levels of structural organization:
1. Primary structure = amino acid sequence
Determined by the genetic code of the mRNA.
2. Secondary structure = folding and twisting of a single polypeptide chain.
Result of weak H-bonds and electrostatic interactions
e.g., -helix (coiled) and -pleated sheet (zig-zag).
• Tertiary structure = three dimensional shape (or conformation) of a polypeptide chain.
Function of R groups contained in the polypeptide.
1. Quaternary structure = association between polypeptides in multi-subunit proteins (e.g., hemoglobin).
Occurs only with two or more polypeptides.
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Fig. 6.4
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Figure 5.0 Spider’s web made of protein
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Figure 5.23 The quaternary structure of proteins
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Final Conformation
3-D shape determined by primary sequence ---> interactions -->spontaneous protein folding
Functional domains
Ultimately protein shape is determined by:
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Changes in Protein Conformation DENATURE - change in shape
due to change in:
• temperature• pH• salt concentration
WEAK BONDS BROKEN
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Changes in Protein Conformation
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Nucleic Acids Information
molecules
DNA(ds) & RNA(ss)
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Nucleotides monomers• Nitrogen base - 2 kinds
• Pentose sugar - 2 kinds
• Phosphate group bonded to 5’ C
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Linkages •Phosphodiester bonds•H-bonds
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Biofunction of Nucleic
Acids
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Additional Nucleotides
ATP NAD FAD Look up their chemical
structures and explain why they belong in this category