Protein Structure - 5.4 Flashcards

1
Q

Functions of Proteins

A

Defense, enzymes, structure, movement, signaling, transport, regulation

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2
Q

monomers of protein

A

amino acid

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3
Q

polymer of protein

A

peptides, polypeptides, proteins

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4
Q

structure composed of

A

alpha carbon, carboxyl (cooh) group, amino (nh2) group, R group

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5
Q

Some r groups are hydrophobic…so they’re

A

nonpolar

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6
Q

Some r groups are hydrophilic…so they’re

A

polar

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7
Q

Neg charged side chain means

A

side chain is acidic
coo
hydrophillic

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8
Q

Pos charged side chain means

A

side chain is basic
amino
hydrophillic

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9
Q

polymerization of amino acids is

A

the formation of a peptide bond (covalent bond)

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10
Q

Polymerization occurs on

A

ribosomes

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11
Q

Primary structure

A

sequence of amino acids

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12
Q

secondary structure

A

coils + folds in the polypeptide chain (bc H bonds between backbone atoms)
Flexible A helices and rigid B sheets

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13
Q

tertiary structure

A

-interactions among various side chains (R groups)
folds into specific 3D, compacted shape
-interactions among R groups of amino acids stabilizes tertiary structure

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14
Q

quaternary structure

A

when a protein consists of multiple polypeptide chains

hemoglobin

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15
Q

disulfide bridges occur between ___ do what?

A

cysteines

stabilizes the protein structure

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16
Q

interactions between polypeptides are

A

NONcovalent

17
Q

protein structure influenced by

A

temperature, pH, salt concentration

18
Q

what makes the protein inactive

A

destroying weak bonds/interactions that maintain 3D structure

19
Q

bond between amino acids

A

peptide bond

20
Q

tertiary structure - ionic bonds form between

A

basic and acidic amino acids

ex: lysine and glutamic acid

21
Q

lysozyme

A

enzyme that helps prevent infection by biding to and destroying specific molcules on the surface of bacteria

22
Q

Folding of the chain influenced by

A

formation of various bonds between parts of the chain

23
Q

amino acids with non polar (hydrophobic) side chains end up

A

at the core of the protein (away from water)

called hydrophobic interactions

24
Q

Cluster of hydrophobic side chains held together by

A

van der waals interactions

25
Q

____ between polar side chains

A

Hydrogen bonds

26
Q

_____ between + and - charged side chains

A

ionic bonds

27
Q

denaturation

A

protein unravels and loses its native shape

inactive