amino acids and proteins Flashcards

(36 cards)

1
Q

what are the 4 constituents of an amino acid?

A

-amino group
-carboxyl group
-single hydrogen
-side chain (R)

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2
Q

what is the backbone of the amino acid?

A

N-C-C

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3
Q

what are the characteristics of non-polar amino acids?

A

-hydrophobic
-help the protein fold and create hydrophobic exclusion or Van der Waals attraction

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4
Q

what are the characteristics of polar uncharged amino acids?

A

-tend to make H-bond
-hydrophilic

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5
Q

what are the characteristics of charged amino acids?

A

-have a side chain that can ionize
-opposite charged side chain of amino acids can interact and create ionic bond
-same charges side chains are repelled by each other

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6
Q

what are characteristics of amino acids that have benzene ring (non-polar)?

A

-non-polar side chain
-hydrophobic
-hydrophobic exclusion or Van der Waals attraction

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7
Q

what are characteristics of amino acids that have benzene ring (polar)?

A

-polar due to hydroxyl functional group (phenol)
-hydrophilic
-arrange themselves towards water molecules, create H-bond

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8
Q

what are characteristics of amino acids that have benzene ring (charged)?

A

-charged due to NH+ in ring
-can create ionic bond (oppositely charged)
-if same charged, will repel

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9
Q

what is the special function of methionine?

A

it is always the first amino acid of a polypeptide in eukaryote and archaea

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10
Q

what is the special function of proline?

A

it induces a kink in the alpha helix

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11
Q

what is the special function of cysteine?

A

-contains a side chain with sulfhydryl, which will link together to create disulfide bridge
-disulfide bridge is a type of covalent bond (strongest bond between side chains)

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12
Q

what are the polymers of amino acids?

A

polypeptides composed of monomers of unbranched amino

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13
Q

what is a protein made out of?

A

one or more polypeptides and can only be called a protein if the polypeptide(s) have a function

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14
Q

what is the name of the bond formed between the amino end and carboxyl end of two adjacent amino acids?

A

peptide bond

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15
Q

true or false: the peptide bond is planar and does not permit rotation

A

true

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16
Q

can rotation occur along the c(alpha)-c bond?

A

yes (it makes the side chain (R) be on the same or opposite side)

17
Q

what is the primary structure of an amino acid?

A

it is the sequence of amino acids linked together by peptide bonds

18
Q

what is the secondary structure of amino acids?

A

it is the interaction of atoms in the peptide backbone (NCC):
-H-bond between amino acids of the backbone

19
Q

what are the two structures that are part of the secondary structure level of an amino acid?

A

-alpha helix
-beta pleated sheet: always composed of 2+ beta strands

20
Q

what are unstructured regions?

A

they are regions between secondary structures

21
Q

what is the tertiary structure of an amino acid?

A

it is the 3D structure formed by the interaction between the side chains (R) of the other amino acids and also with the environment

22
Q

true or false: only a polypeptide with a tertiary structure can form a functioning protein

23
Q

what is the quaternary structure of an amino acid?

A

it is the arrangement of 2+ polypeptide chains in a functional protein

24
Q

what are motifs?

A

-they are similarities between otherwise dissimilar proteins
-also called super-secondary structures

25
describe the motif helix-turn-helix
-major structural motif capable of binding DNA -each monomer incorporates two alpha-helices, joined by a short strand of amino acids, that bind to the major groove of the DNA -occurs in many proteins that regulate gene expression
26
describe the motif beta barrel
-beta sheet folded around to form a tube -involved in membrane transport
27
describe the motif beta-alpha-beta
-contains two beta sheets which are connected by an alpha helix -creates a fold/crease at the core of nucleotide binding site in a wide variety of proteins e.g. FAD, NAD+, NADP+
28
true or false: motifs have not been useful to determine the function of unknown proteins
false
29
what are domains?
-functional units within a larger structure -can be thought of as a substructure within the tertiary structure of a protein -most proteins are made up of multiple domain that perform different parts of the protein's function
30
name the different protein functions
-enzyme catalysis -defense -transport -support -motion -regulation
31
what are some environmental factors that can change the structure and function of proteins?
-temperature -pH -organic solvent
32
how will temperature affect the shape of a protein?
-function of a protein will be outside if the temperature is outside of its nominal range
33
how will pH affect the shape of a protein?
-will cause disruption of the ionic bond -will cause disruption of the hydrogen bond
34
how will high ion concentration (salt) affect the shape of a protein?
-disrupts ionic bonds
35
what is the denaturation of a protein?
-environmental exceed the limitation of a protein, the secondary, tertiary, and quaternary bonds are overcome -the protein will no longer function, the damage is irreversible
36
explain the denaturation of keratin
-composed of long alpha-helix with hydrophobic amino acids -lots of disulfide bonds -permanent wave is made by reducing the disulfide bond and generating a new one