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AP Biology
Discuss the following with your group and be prepared to discuss
with the class
1. Why is the shape of a molecule important?
2. How is a covalent bond different from ionic?
3. How are hydrogen bonds different from covalent?
We are beginning our first Unit today: Bio-Molecules
Right now, the test is set for Tuesday, Sept 17th
Functional groups-parts of organic molecules that are
involved in chemical reactions
They give organic molecules distinctive properties
hydroxyl amino
carbonyl (ketones and aldehydes) sulfhydryl
carboxyl phosphate
H2O
HO
HO H
H HHO
Polymers- long molecules built by linking repeating
building blocks in a chain monomers
building blocks repeated small units
covalent bonds
H2O
HO
HO H
H HHO
How to build a larger Bio-molecule
Dehydration Synthesis (also called Condensation Reaction)
joins monomers by “taking” H2O out one monomer donates OH–
other monomer donates H+ together these form H2O
requires energy & enzymes
enzymeThis is an example of an
Anabolic, endergonic
reaction.
H2O
HO H
HO H HO H
How to break down a larger molecule
Hydrolysis (also called Digestion)
use H2O to breakdown polymers reverse of dehydration synthesis takes off one monomer at a time
H2O is split into H+ and OH–
H+ & OH– attach to ends
requires enzymes releases energy enzyme
This is an example of an
Catabolic, exergonic
reaction.
Bio-Molecules Large organic molecules formed by
smaller molecules bonding together macromolecules
4 major classes of macromolecules: carbohydrates lipids proteins nucleic acids
AP Biology 2008-2009
ProteinsMultipurpose
molecules
Proteins
Various functions: enzymes (speed up metabolism) structure physical stability and movement
(keratin-hair/nails/skin, collagen-bones/cartilage/tendons, myosin-muscles)
transport (hemoglobin- in red blood cells, proteins in cell membranes)
cell communication/regulatory signals (insulin & other hormones) receptors
defense (antibodies/recognize foreign invaders)
storage (hold amino acids for later use)
- Most structurally & functionally diverse group
Amino acids
central carbon Two functional groups:
carboxyl group (acid) amino group
R group (side chain) variable group that is
different for each amino acid gives unique chemical
properties to each amino acid like 20 different letters of an
alphabet can make many words (proteins)
—N—H
HC—OH
||O
R
|—C—
|
HProtein monomer (building block)
Peptide Bonds – Linking of Amino Acids
Effect of different R groups:Nonpolar amino acids
nonpolar & hydrophobic
Effect of different R groups:Polar amino acids
polar or charged & hydrophilic
Building proteins Peptide bonds
covalent bond between NH2 (amino) of one amino acid & COOH (carboxyl) of another
C–N bond
peptidebond
dehydration synthesisH2O
Building proteins Polypeptide chains have direction
N-terminus = NH2 end C-terminus = COOH end repeated sequence (N-C-C) is the
polypeptide backbone
Protein structure & function
hemoglobin
Function depends on structure 3-D structure
twisted, folded, coiled into unique shape
collagen
pepsin
Primary (1°) structure Order of amino acids in chain
amino acid sequence determined by genes (DNA)
slight change in amino acid sequence can affect protein’s structure & its function even just one amino acid change
can make all the difference!
(Example of structure determining function) Sickle Cell Anemia
What type of mutation is
this?
Secondary (2°) structure “Local folding”
folding along short sections of polypeptide interactions between
adjacent amino acids H bonds
weak bonds between R groups
forms sections of 3-D structure helix pleated sheet
Tertiary (3°) structure “Whole molecule folding”
interactions between distant amino acids and R groups
Quaternary (4°) structure More than one polypeptide chain bonded
together
collagen = skin & tendons hemoglobin
Protein denaturation Unfolding a protein
conditions that disrupt H bonds and ionic bonds temperature pH salinity
alter 2° & 3° structure alter 3-D shape
destroys functionality some proteins can return to their functional shape
after being denatured, many cannot
Enzymes a type of protein that acts as a catalyst, speeding
up chemical reactions
H2O
Substrate(sucrose)
Fructose
Glucose
Some enzymes require other atoms or molecules in order to
function:
-Cofactors: inorganic ions, such as iron, copper, or zinc that bind to
enzymes in order to help break down specific substances.
-Coenzymes: organic molecules that are required by certain enzymes to
carry out catabolic reactions.