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AGBI 410 > Day 7 > Flashcards

Day 7 Flashcards

1
Q

overall three dimensional arrangement of all th atoms in a protein

A

tertiary structure

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2
Q

what holds segments in position in tertiary structure

A

weak interactions and covalent bonds

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3
Q

arrangement of 2+ separate polypeptide chains in 3D complexes

A

quaternary structure

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4
Q

how many major types of proteins based on polypeptide chains

A

4a

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5
Q

arranged in long strands or sheets

A

fibrous proteins

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6
Q

folded into a spherical or globular shape

A

globular proteins

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7
Q

embedded in a hydrophobic lipid membranea

A

membrane proteins

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8
Q

lacking stable tertiary strucurres

A

intrinsically disordered proteins

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9
Q

givers strength and or flexibility to structure s

A

fibrous proteins

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10
Q

simple repeating element of secondary structure

A

fibrous proteins

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11
Q

example of right handed alpha helix

A

alpha kertatin

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12
Q

main protein in silk

A

fibroin

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13
Q

predominately beta sheets conformation

A

fibroin

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14
Q

what is fibroin rich n

A

alanine and glycine

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15
Q

what is fibroin stabilized by

A

hydrogen bonding and van der waals interactions

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16
Q

found in connective tissue

A

collagen

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17
Q

what is the secondary structure of collagen

A

left handed helix

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18
Q

what is tertiary and quaternary structure of collagen

A

right handed twisting of 3 separate polypeptides

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19
Q

what is caused by lack of vitamin C

A

scurvy

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20
Q

fold back on each other, more compact than fibrous proteins

A

globular proteins

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21
Q

enzymes, transport proteins, motor proteins, regulatory proteins, immunoglobins are all what

A

globular proteins

22
Q

lack definable structure

A

instrinsically disordered proteins

23
Q

often lack a hydrophobic core

A

intrinsically disordered proteins

24
Q

high densities of charged residues and proline

A

intrinsically disordered proteins

25
Q

motif = what

A

fold

26
Q

recognizable folding pattern involving 2+ elements of secondary structure and the connections

A

motif/fold

27
Q

assembly of multiple peptide subunits, what structure

A

quaternary structure

28
Q

repeating structural unit

A

protomer

29
Q

multisubunit protein

A

oligomer/multimer

30
Q

loss of 3D structure sufficient to cause loss of function

A

denaturation

31
Q

what can cause denaturation

A

heat, pH extremes, miscible solvents, certain solutes, detergents

32
Q

what does denaturation often lead to

A

protein precipitation

33
Q

process by which certain denatured globular proteins regain their native structure and biological activity

A

renaturation

34
Q

can all proteins undergo renaturation

A

no

35
Q

2 kinds of protein folding

A

spontaneous and assisted folding

36
Q

based on amino acid r group interactions, what folding type

A

spontaneousg

37
Q

guided by chaperone proteins

A

assisted folding

38
Q

binds to hydrophobic regions

A

HSP 70

39
Q

protein complexes assign in protein folding

A

chaperonins

40
Q

misfolded protein

A

prion

41
Q

what dictates protein function

A

structure of the protein

42
Q

many proteins require what to function

A

binding to a ligand

43
Q

anything that binds the protein at a specific site

A

ligand

44
Q

protein functions can either be grouped as what or what

A

catalytic or noncatalytic

45
Q

example of non catalytic protein functiosn

A

oxygen binding proteins like myoglobin and hemoglobin

46
Q

what group do myoglobin and hemoglobin require

A

heme

47
Q

consists of complex organic ring structure with a bound Fe2+ atom

A

heme

48
Q

highly conserved tertiary structure with 8 alpha helical segments connected by bends

A

globins

49
Q

most globes function in what

A

O2 transport or storage

50
Q

153 residues and 1 molecule of heme

A

myoglobin

51
Q

oxygen carrier in the muscle

A

myoglobin

AGBI 410 (26 decks)

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