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

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2
Q

bronsted acid

A

proton donor

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3
Q

bronsted base

A

proton acceptor

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4
Q

concentration of H+ in pure water at 25*C

A

1.0 E-7 M

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5
Q

Kw

A

1.0 E-14

H*OH

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6
Q

narrow range pH paper

A

2 pH units

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7
Q

wide range pH paper

A

12 pH units

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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

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9
Q

titration

A

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

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10
Q

equivalence point

A

point in titration in which acid is exactly neutralized

moles acid = moles base

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11
Q

pH = pKa

A

inflection point

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12
Q

BUFFER PROBLEM 3

A

learn it

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13
Q

first level of p structure

A

primary structure; linear sequence of AA linked by peptide bonds

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14
Q

second level of p structure

A

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

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15
Q

secondary structure elements

A

parallel/antiparallel b sheets
a-helices
b-turns

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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
Q

proteins conformation is stabilized by

A

weak molecular interactions (van der waals, H bonding, hydrophobic interactions, ionic interactions)

covalent and noncovalent contribute to native state

26
Q

most stable conformation of protein will have

A

max weak interactions

easily disrupted; only marginally stable

27
Q

charged or polar AA on

A

surface of a protein

promote appropriate folding by interacting w water molecules via h bonds

28
Q

h bonds

A

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
Q

hydrophobic interactions

A

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
Q

soluble prtoein

A

hydrophobic residues in interior

h bonds maximized