Proteins Flashcards

1
Q

Amino Acid general structure

A

R group
Amino - alpha carbon - carboxyl
H

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2
Q

How do peptide bonds form?

A

Dehydration synthesis (water out, peptide bond formed) between Amino and Carboxyl

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3
Q

Different protein functions (8)

A

Enzymatic, Defensive, Storage, Transport, Hormonal, Receptor, Contractile/Motor, Structural

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4
Q

Enzymatic protein

A

Function: Selective acceleration of chemical reactions

Example: Digestive enzymes

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5
Q

Defensive protein

A

Function: Protect against disease

Example: Antibodies

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6
Q

Hormonal protein

A

Function: Coordinate organisms activities

Example: Insulin tells body to take up glucose

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7
Q

Receptor protein

A

Function: Respond to chemical stimuli

Example: Receptors

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8
Q

Contractile and motor proteins

A

Function: Movement

Example: Actin and moving make muscle contractions

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9
Q

Structural protien

A

Function: Support

Example: Keratin is protein of hair, horns, feathers. Also collagen

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10
Q

Globular protien

A

A roughly spherical shaped protien

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11
Q

Fibrous protien

A

3 polypeptides coiled like long rope

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12
Q

Primary structure

A

Linear chain of amino acids

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13
Q

Secondary Structure

A

alpha helix shape or a beta pleated shape caused by hydrogen bonds between the polypeptide backbone

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14
Q

Alpha helix secondary structure

A

Coil shape held by hydrogen bonds between every fourth amino acids

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15
Q

Beta pleated sheet

A

Two or more parallel polypeptide chains connected by hydrogen bonds

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16
Q

Tertiary Structure

A

3D dimensional shape of protein made from interactions between the side chains

17
Q

TS: Hydrogen bond

A

Attraction between polar side chains
(Have OH, NH)

18
Q

TS: hydrophobic interaction

A

Nonpolar amino acids bond together, causing van Der Waals interaction
(CH or just H. Also 2 ring NH)

19
Q

TS: Ionic bond

A

(+ or - charge)

20
Q

TS: Disulphide bridge

A

-SH plus -SH
Equal S-S

21
Q

Quaternary Structure

A

Protien made of more than one polypeptide (multiple TS put together)

22
Q

Enzyme mechanism to make reactions easier and faster

A

Align reactants when multiple, stretch substrates to encourage breaking of bonds, better microenviroment, directly participate in reactions.

23
Q

Cofactor

A

Non-organic enzyme helper

24
Q

Coenzyme

A

Organic enzyme helper

25
Q

Hydrophobic interactions use what side chains (R Group)?

A

Nonpolar Hydrophobic, H and the ones with CH

26
Q

Ionic bonds use what side chains (R groups)?

A

Charged hydrophilic, + and - charged ones

27
Q

Hydrogen bonds use what side chains?

A

Polar Hydrophilic, OH

28
Q

Hydrogen bonds use

A