Day 7 Flashcards

(51 cards)

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
motif = what
fold
26
recognizable folding pattern involving 2+ elements of secondary structure and the connections
motif/fold
27
assembly of multiple peptide subunits, what structure
quaternary structure
28
repeating structural unit
protomer
29
multisubunit protein
oligomer/multimer
30
loss of 3D structure sufficient to cause loss of function
denaturation
31
what can cause denaturation
heat, pH extremes, miscible solvents, certain solutes, detergents
32
what does denaturation often lead to
protein precipitation
33
process by which certain denatured globular proteins regain their native structure and biological activity
renaturation
34
can all proteins undergo renaturation
no
35
2 kinds of protein folding
spontaneous and assisted folding
36
based on amino acid r group interactions, what folding type
spontaneousg
37
guided by chaperone proteins
assisted folding
38
binds to hydrophobic regions
HSP 70
39
protein complexes assign in protein folding
chaperonins
40
misfolded protein
prion
41
what dictates protein function
structure of the protein
42
many proteins require what to function
binding to a ligand
43
anything that binds the protein at a specific site
ligand
44
protein functions can either be grouped as what or what
catalytic or noncatalytic
45
example of non catalytic protein functiosn
oxygen binding proteins like myoglobin and hemoglobin
46
what group do myoglobin and hemoglobin require
heme
47
consists of complex organic ring structure with a bound Fe2+ atom
heme
48
highly conserved tertiary structure with 8 alpha helical segments connected by bends
globins
49
most globes function in what
O2 transport or storage
50
153 residues and 1 molecule of heme
myoglobin
51
oxygen carrier in the muscle
myoglobin