Structure of proteins II Flashcards

1
Q

how are beta strands held together

A

interchain hydrogen bonding of the backbone C=O and N-H groups

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2
Q

antiparallel beta sheets

A

adjacent strands run in opposite directions

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3
Q

parallel beta sheets

A

adjacent strands run in same directions

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4
Q

what are reverse turns stabilized by

A

hydrogen bonding, salt bridges, metal ions, disulfide bonds

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5
Q

what is often found in reverse turns

A

proline and glycine

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6
Q

what is tertiary structure

A

3D folded structure

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7
Q

prosthetic groups

A

organic molecules that are permanently bound to the protein

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8
Q

apoproteins

A

lack prosthetic group whilst the final functional molecule is said to have the native strucutre

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9
Q

what is unqiue about myoglobin

A

has high affinity for oxygen
heme group contains an Fe2+ ion that is required for oxygen binding
secondary structural elements are all alpha helices

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10
Q

what are some ways that the native structure of proteins can be denatured

A

incrased temp
detergents
pH extreme
agents like urea and guanidinium hydrochloride

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11
Q

how does denaturing work

A

disrupt non-covalent bonds that maintain folded conformation of the protein

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12
Q

how does protein foldign occur

A

favored pathways in a cooperative manner

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13
Q

what is protein folding driven by in an aqueous environement

A

strong tendency of hydrophobic residues to be excluded from water

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14
Q

forces that contribute to stabilizing protein structure

A

cystine disulfide bridges
hydrogen bonding
ionic interactions
hydrophobic forces

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15
Q

where are salt bridges and hydrogen bonding usually taking place

A

internal portion of molecule or interfaces btwn polypeptide chains

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16
Q

where are hydrophobic amino acids suually

17
Q

prion

A

proteiancous infection partical

18
Q

examples of prion diseases

A

creutzfeldt jakob
kuru
vCJD

19
Q

how is kurur transmitted

A

funeral rites involving cannablism

20
Q

how is CJD spread

A

spontaneous and inherited

21
Q

how is vCJD spread

A

tranmitted

BSE-infected cow

22
Q

what secondary structure predominates in prions

A

beta sheet

23
Q

what aggregates in parkinsons

A

alpha synuclein

24
Q

Hb is a tetramer of what

A

2 alpha-globin and 2 b-globin subunits

25
what does the Hb tetramer form form assocation of
2 alpha-beta dimers
26
what are the cohesive forces acting in Hb
hydrophbic, hydrogen bonding, salt bridge
27
when does Hb not bind O2 efficiently
low O2 conc
28
where does Hb bind O2 efficiently
high O2 conc
29
when does myoglobin bind O2 qwith high affinity
low O2
30
what is the shape of Hb binding curve
sigmoid
31
what is the shape of myoglobin binding curve
hyperbolic
32
what is the tight conformation of deoxygenated Hb
T form
33
what is happening during the T form
valine residue partially blocks the O2 binding site
34
what is the high affinity Hb form
R-form
35
how does 2,3 BPG affect Hb
stabilizes T form, reduces o2 affinity
36
what happens when H+ bindings specific histdiines in Hb
form salt bridges, stabilizes T form, promotes O2 release