Proteins Flashcards
Amino Acid general structure
R group
Amino - alpha carbon - carboxyl
H
How do peptide bonds form?
Dehydration synthesis (water out, peptide bond formed) between Amino and Carboxyl
Different protein functions (8)
Enzymatic, Defensive, Storage, Transport, Hormonal, Receptor, Contractile/Motor, Structural
Enzymatic protein
Function: Selective acceleration of chemical reactions
Example: Digestive enzymes
Defensive protein
Function: Protect against disease
Example: Antibodies
Hormonal protein
Function: Coordinate organisms activities
Example: Insulin tells body to take up glucose
Receptor protein
Function: Respond to chemical stimuli
Example: Receptors
Contractile and motor proteins
Function: Movement
Example: Actin and moving make muscle contractions
Structural protien
Function: Support
Example: Keratin is protein of hair, horns, feathers. Also collagen
Globular protien
A roughly spherical shaped protien
Fibrous protien
3 polypeptides coiled like long rope
Primary structure
Linear chain of amino acids
Secondary Structure
alpha helix shape or a beta pleated shape caused by hydrogen bonds between the polypeptide backbone
Alpha helix secondary structure
Coil shape held by hydrogen bonds between every fourth amino acids
Beta pleated sheet
Two or more parallel polypeptide chains connected by hydrogen bonds
Tertiary Structure
3D dimensional shape of protein made from interactions between the side chains
TS: Hydrogen bond
Attraction between polar side chains
(Have OH, NH)
TS: hydrophobic interaction
Nonpolar amino acids bond together, causing van Der Waals interaction
(CH or just H. Also 2 ring NH)
TS: Ionic bond
(+ or - charge)
TS: Disulphide bridge
-SH plus -SH
Equal S-S
Quaternary Structure
Protien made of more than one polypeptide (multiple TS put together)
Enzyme mechanism to make reactions easier and faster
Align reactants when multiple, stretch substrates to encourage breaking of bonds, better microenviroment, directly participate in reactions.
Cofactor
Non-organic enzyme helper
Coenzyme
Organic enzyme helper
Hydrophobic interactions use what side chains (R Group)?
Nonpolar Hydrophobic, H and the ones with CH
Ionic bonds use what side chains (R groups)?
Charged hydrophilic, + and - charged ones
Hydrogen bonds use what side chains?
Polar Hydrophilic, OH
Hydrogen bonds use