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Biochemistry I > FINAL - CH 4 > Flashcards

FINAL - CH 4 Flashcards

1
Q

oligopeptides

A

Short polypeptides less than 40 amino acids in length

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2
Q

Enantiomers

A

Molecules that are non-superimposable mirror images of one another

Able to rotate light (optically active)

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3
Q

Most AA’s are _____ besides ____

A

Chiral

Glycine

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4
Q

Each AA has a ____ and ____ form

A

D and L

L are used to build proteins/only found in humans

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5
Q

the only amino acid that can form disulfide bonds

A

Cysteine - stabilizes 3D structure

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6
Q

Isoelectric Point

A

pH at which the amino acid is neutral

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7
Q

Electrically neutral molecule with positive (amino) and negative (carboxyl groups)

A

Zwitterion

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8
Q

Average molecular weight if an AA

A

110 g/mol OR dalton

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9
Q

How to find PI if there are two Pka’s

A

Take average

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10
Q

How to find PI if there are 3 Pka’s

A

Draw the structure starting form fully protonated to fully deprotonated.. take the average of the two Pka’s where the molecule is neutral

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11
Q

Pka is the pH where:

A

half the molecules of an amino acid in solution have side chains that are charged. Half are uncharged

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12
Q

stimulates water resorption by kidneys and

increases blood pressure

A

Vasopressin

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13
Q

stimulates uterine contractions during childbirth – induces labor

A

Oxytocin

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14
Q

the angle of rotation around the N-Cα

A

phi (φ)

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15
Q

the angle of rotation around the Cα–C

A

psi (Ψ)

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16
Q

Secondary structures

A

β strands

α helices

β turns

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17
Q

α helices

A

Right handed

Stabilized by hydrogen bonding

Has 3.6 residues per turn

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18
Q

H bonding and alpha helices

A

N + 4 rule

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19
Q

α helices have ______ H bonding

A

Intrastranded

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20
Q

The most common location for an α-helix

A

along the outside of the protein, with one side of helix facing the solution and the other side facing the hydrophobic interior

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21
Q

β turns

A

Connect two β strands in antiparallel β sheet

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22
Q

β sheets have ______ H bonding

A

Interstranded

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23
Q

β strands can interact in two ways to form a pleated sheet: _____________

A

parallel and antiparallel

24
Q

Antiparallel β sheets H bonds

A

More narrow and more stable

25
Q

Parallel β sheets H bonds

A

Equally spaced, H bonds are at an angle

26
Q

_____ is made from β sheets

A

Silk

27
Q

Beta Turns

A

Type I: Turn with the carbonyl oxygen inward

Type II: Turn with the carbonyl oxygen facing outward

28
Q

_______ Observed in tertiary

structure

A

Disulfide bonds

29
Q

First protein structure determined

A

Myoglobin

Largely α helical in structure

30
Q

Tertiary structures protein folds

A 
Four helix bundle fold
Greek key fold
Rossmann fold
TIM barrel fold (also called an α/β barrel)
FERM domain fold
31
Q

Homodimer

A

Simplest quaternary structure

Contains two identical protein subunits

32
Q

Heterodimer

A

Contains subunits from different gene products

33
Q

Hemoglobin

A

Has four polypeptide chains, non-covalently bound

Mostly α-helical

NO beta strands

34
Q

Fibrous Proteins

A

Keratin

Silk

Collagen

35
Q

Collagen Consists of ____________________

A

three intertwined left-handed helices

36
Q

Globular Proteins

A

Spherical proteins that consist of multi subunit protein complexes

EX: immunoglobulins

37
Q

Most abundant protein in the human body

A

Collagen

38
Q

Four major classes of structures

A

Predominately α helices

Predominately β heet

α /β combined

Mixed α & β

39
Q

3 models for protien folding

A

Hydrophobic collapse
Nucleation model
Framework model

40
Q

Chaperone Proteins

A

Proteins that facilitate the formation of stable 3D

structures

41
Q

Chaperone Proteins Functions:

A

Help newly synthesized proteins fold properly

Rescue misfolded proteins

Disrupt protein aggregates

42
Q

Two types of chaperone proteins

A

Clamp type (HSP 70)

Chamber type (GroEL-GroES protein complex)

43
Q

Both types of chaperones bind to misfolded proteins and use _______ to facilitate correct folding

A

ATP hydrolysis

44
Q

GroEL has _____ subunits

A

14

45
Q

pH < Pka

A

Protonation

46
Q

pH > Pka

A

Deprotonation

47
Q

Tm

A

Transition curve mid point - half of proteins are unfolded

Tm is on X axis

48
Q

Alzheimers disease

A

caused by the aggregation of Aβ peptides

Aggregates are referred to as β-amyloid plaques

49
Q

bps per turn in B DNA

A

10.5 bp/turn

50
Q

bps per turn in A DNA

A

11 bp/turn

51
Q

bps per turn in Z DNA

A

12 bp/turn

52
Q

The isoelectric point is where:

A

AA has no charge

53
Q

_____ is not found in Alpha helices

A

Proline

54
Q

Angles in beta sheet

A

+psi

-phi

55
Q

Angles in alpha helix

A
  • psi

- phi

Biochemistry I (13 decks)

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