Biochem Final part 1 Flashcards

1
Q

Hydrophobic

A

water-fearing

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

hydrophobic effect

A

the energetic preference of nonpolar molecular surfaces to interact with other nonpolar molecular surfaces and thereby to displace water molecules from the interacting surfaces

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Hydrophilic

A

water-loving

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Amphoteric

A

they can react either as acids or bases, depending on the circumstances

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Isoelectric point

A

the pH at which the net electric charge is zero

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

zwitterion

A

a functional group molecule in which at least one has a positive electrical charge and one a negative electrical charge.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

primary structure

A

covalent bonds linking amino acid residues in a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

secondary structure

A

recurring structural patterns
-ɑ-helix, β-sheets, β-turn, random coils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

tertiary structure

A

3D folding of polypeptide
-determined by amino acid sequence
-hydrogen bonds between nearby amino acid residues
- salt bridges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

quaternary structure

A

2+ polypeptide subunits

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

protein domain

A

part of a polypeptide chain that is independently stable or could undergo movements as a single entity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

motif

A

recognizable folding pattern involving 2+ elements of 2° structures & the connection(s)
b-a-b loop or b barrel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Intrinsic disorder proteins

A

-Lack of definable structure
-Often lack a hydrophobic core
-High densities of charged residues (Lys, Arg, Glu) and Pro
-Facilitates protein interactions with multiple binding partners

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Denaturation

A

loss of three-dimensional structure sufficient to cause loss of function
- can happen by heat, pH extremes, detergents, strong acids/bases, organic solvents

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

native conformation

A

the arrangement of all atoms contained in the protein in a conformation that is stable and functional
thermodynamically the most stable, therefore, lowest free energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

enzyme

A

A biomolecule, either protein or RNA, that catalyzes a specific chemical reaction

17
Q

substrate

A

the molecule that is bound to the active site and acted upon by the enzyme

18
Q

Active site

A

provides a specific environment in which a given reaction can occur more rapidly

19
Q

allosteric site

A

an effector binding site within enzymes, distinct from the active site, that
allows molecules to either activate or inhibit (or turn off) enzyme activity

20
Q

Pre-steady state

A

the initial transient period during which ES builds up

21
Q

steady state

A

the period during which [ES] and other intermediates remain constant

22
Q

Saturation effect

A

occurs at Vmax, when virtually all the enzyme is present as the ES complex
- Further increases in [S] do not affect rate

23
Q

Km vs Kcat

A

Km: Michaelis constant, characteristic of the enzyme and the substrate under s[ecific conditions
Kcat: limiting rate of any enzyme-catalyzed reaction at saturation

24
Q

V0 vs Vmax

A

V0: initial velocity
Vmax: maximum velocity

25
Q

Stereoisomer

A

each of two or more compounds with the same molecular formula,
differing only in the spatial arrangement of their atoms

26
Q

enantiomer

A

stereoisomers that are mirror images

27
Q

diastereomer

A

stereoisomers that are not enantiomers (D (OH to the right) and L(OH to the left))

28
Q

aldose

A

sugar with the carbonyl group is at the end of the carbon chain (in an aldehyde group)

29
Q

Hemiacetal (/hemiketal)

A

Ring formation that occurs because aldehyde and ketone groups react reversibly with hydroxyl groups in an aqueous solution

30
Q

ketose

A

sugar with the carbonyl group is at any other position (in a ketone group)

31
Q

acetal (/ketal)

A

Glycoside formation: hemiacetals and hemiketals react with alcohols to form the corresponding acetal and metal - no OH instead two OR groups

32
Q

pyranose

A

six-membered rings are pyranoses ex: fructose (monosaccharide cyclization)

33
Q

furanose

A

Five-membered rings are called furanoses

34
Q

Anomer (alpha and beta)

A

The two possible diastereomers that form because of cyclization
are called anomers; up (above ring, β) or down (below ring, ɑ)