Practical Flashcards

1
Q

autoionization of water

A

ability of water to act as bronsted acid or bronsted base

water donating proton to another water molecule

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

bronsted acid

A

proton donor

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

bronsted base

A

proton acceptor

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

concentration of H+ in pure water at 25*C

A

1.0 E-7 M

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

Kw

A

1.0 E-14

H*OH

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

narrow range pH paper

A

2 pH units

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

wide range pH paper

A

12 pH units

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

pH meter

A

glass electrode connected to meter
voltage produced depends on pH of solution
electrical potential produced is linear function of pH

voltage produced is read by the meter and calibrated to .01pH units

must be standardized with buffer solutions with known pHs

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

titration

A

measured amounts of base are added to measured amount of acid or vice versa

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

equivalence point

A

point in titration in which acid is exactly neutralized

moles acid = moles base

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

pH = pKa

A

inflection point

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

BUFFER PROBLEM 3

A

learn it

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

first level of p structure

A

primary structure; linear sequence of AA linked by peptide bonds

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

second level of p structure

A

sterical arrangement of amino acid residues in specific parts of polypeptide chain

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

secondary structure elements

A

parallel/antiparallel b sheets
a-helices
b-turns

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

tertiary structure

A

3D structure of pp chain

17
Q

function of protein is dependent on

A

correct 3D structure (tert)

18
Q

2 abundant classes of proteins based on tert structure

A

fibrous

globular

19
Q

fibrous proteins

A

simple, repeating elements of secondary structure and have structural roles

silk fibroin

20
Q

silk fibroin

A

layers of antiparallel b-sheets

21
Q

globular prtoeins

A

several types of secondary structure in same pp chain

myoglobin

22
Q

quaternary structure

A

protein has 2 or more pp subunits that can interact w each other

hemoglobin

23
Q

protein native state

A

functional folded conformation

lowest Gibbs free energy

24
Q

native state represents

A

most thermodynamically stable state

25
proteins conformation is stabilized by
weak molecular interactions (van der waals, H bonding, hydrophobic interactions, ionic interactions) covalent and noncovalent contribute to native state
26
most stable conformation of protein will have
max weak interactions | easily disrupted; only marginally stable
27
charged or polar AA on
surface of a protein promote appropriate folding by interacting w water molecules via h bonds
28
h bonds
between atoms on 2 diff side chains water and AA on surface carbonyl and amide groups in peptide backbone that give rise to a-helix and b-strand conformations
29
hydrophobic interactions
major driving force for native fold forms solvation layers solvation layer is highly ordered; unfavorable decrease in entropy of water nonpolar AA cluster together, increases entropy because less solvation
30
soluble prtoein
hydrophobic residues in interior h bonds maximized