Chapter 6- Secondary Structures of Proteins Flashcards

1
Q

What happens in sickle cell?

A

a glutamine is replaced with a valine= alters hemoglobin structures and function.

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2
Q

What does protein function depend on?

A

on protein structure

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3
Q

What is the relationship of protein sequence to function dependent on?

A

the 3D folding of proteins and inferring protein functions from these 3D structures (binding sites, catalytic activities, interactions w/ other molecules)

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4
Q

What are the importance of proteins ?

A

motor proteins, structural components of cells, enzymes, antibodies, hormones, hemoglobin/ myblobin, transport proteins in blood.

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5
Q

What are the 4 levels of protein structure and define them?

A

primary- amino acid linear sequence (from n term to c term) determines structure and function

secondary- regions of regularly repeating conformation of the peptide chain (a-helices ad beta sheet). joined by turns and loops

tertiary- describes shape of fully folded folded polypeptide chain

quaternary- arrangement of two or more polypeptide chains into a multi subunit molecule

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6
Q

What are the first 5 amino acids residues in lysozyme?

A

Lys-Val-Phe-Gly-Arg (2,3,4- hydrophobic-faces in)

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7
Q

What makes polypeptides fold in water into 3D structues? (tertiary )

A

bond rotation within the polypeptide backbone

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8
Q

What causes secondary structure?

A

regularly spaced hydrogen bonds (a-helix, beta sheet, beta turn, loop)

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9
Q

are alpha helices right or heft handed?

A

right handed

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10
Q

describe the a-helix structure. shape? what bonds? between what?

A

cork screw, telephone cord held by H bonds rom -N-H groups and the O- of c+o of the fourth amino acid along chain

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11
Q

what stabilizes the helix ?

A

the H bonds between back bone atoms Not R groups

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12
Q

which way do the r groups of a helix face?

A

perpendicular to helix axis

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13
Q

What is a triple helix?eg.

why are they so strong?

typical of what ?

A

3 polypeptide chain woven together ?
Glycine, Proline, Hydroxyproline, Hydroxylysine

because of the H bonding between -OH groups

collagen, connective tissue, skin, tendons, cartilage (cccts)

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14
Q

Why are helices short and why do they overlap?

A

so they are strong

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15
Q

a-helices are major components of many proteins, connected by turns. some interesting a helices are…

A

small DNA binding helices -
Membrane- spanning helices
amphipathic helices
coiled coils

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16
Q

how are a-helices are major component of small DNA binding helices?

A

fit in the major groove of double stranded DNA

17
Q

how are a-helices are major component of membrane- spanning helices
?

A

they have hydrophobic amino amine in the central region that allow the helices to enter the bilayer

18
Q

how are a-helices are major component of amphipathic helices?

A

the helices have some hydrophilic amino acids on one side and hydrophobic ones on the other side - integral protein.

19
Q

Most amino acids like to in an a-helix except for?

A

Glycine and proline

20
Q

proline is not an amino acid but a?

A

imino acid (secondary amino acid, N-bonded to 2 carbons, not bonded to any H )

21
Q

what do proline residues do?

A

they act as a-helix breakers

22
Q

where are proline residues normally found?

A

at the boundaries of a-helices and in turns

23
Q

describe beta sheets? shape? what bonds?

A

the are like an accordion, they can join distant parts of the protein together due to H-bonds

24
Q

how are beta pleated sheets arranged ?where residues face? bonds? where do r groups extend? eg.

A

the polypeptide chains are side by side and H bonds forms between chains (residues are rotated 180 from neighbour-side chains protrude on opposite ends). R groups extend above and below sheet. Silk

25
Q

beta sheets can be parallel or anti parallel

A

anti= 2 bond close the gap etc.

26
Q

beta sheet unit, what is the super structure they can form?

A

beta strand
beta barrels- strands are twisted and at an incline, r groups stick out on either face. r groups inside the barres are often beta-branched or hydrophobics

27
Q

where do b-sheets fit?

A

In the minor groove of DNA double helix , can also used in DNA binding but are less common