Biochem Flashcards

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1
Q

Where do D amino acids exist

A

prokaryotes

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2
Q

Nonpolar, nonaromatic amino acids

A

glycine, alanine, valine, leucine, isoleucine, methionine, proline

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3
Q

Aromatic amino acids

A

tryptophan, phenylalanine, tyrosine

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4
Q

Polar Amino acids

A

Serine, threonine, asparagine, glutamine, cysteine

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5
Q

Negatively charged amino acids

A

aspartate, glutamate

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6
Q

Positively charged amino acids

A

lysine, arginine, histidine

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7
Q

Nature of amino acid at low PH

A

fully protonated

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8
Q

Nature of Amino acid at high PH

A

fully deprotonated

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9
Q

Nature of Amino Acid at isoelectric point

A

zwitterion

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10
Q

PI of amino acids without charged side chains

A

6

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11
Q

peptide formation is what type of reaction

A

dehydration

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12
Q

conjugated proteins

A

have attached molecules called prosthetic groups which can be metal ions, vitamins, lipids, carbs, or nucleic acids

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13
Q

Oxidoreductase

A

catalyzes REDOX reactions

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14
Q

transferase

A

move a functional group from one molecule to another

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15
Q

hydrolase

A

cleaves with water

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16
Q

lysase

A

cleaves without water

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17
Q

isomerase

A

interconversion of isomers including constitutional isomers and stereoisomers

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18
Q

how do enzymes work

A

by stabilizing the transition state

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19
Q

Michaelis Mentin Plot info

A

plots substrate concentration (x) and reaction velocity (y)
Km value occurs at 1/2 vmax

v = (vmax[s])/(Km+[S])
vmax = [E]kcat
v=(Kcat/Km +[S])[E][S] but at low substrate concentration S can be negated and the equation is v=(Kcat/Km)[E][S]

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20
Q

Lineweaver-Burn Plot info

A

plots 1/v (y) against 1/[S] (x)

x intercept is (-1/Km) Y intercept is (1/vmax)

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21
Q

Catalytic Intensity

A

Kcat/Km

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22
Q

Hills coefficient

A

describes cooperative binding. Above one indicates cooperative binding, below one indicates negative cooperative binding, a value of 1 indicates no cooperative binding

23
Q

Competitive inhibition

A

when inhibitor is similar to subtrate and binds to active site. Can be overcome by adding more substrate. Has no effect on vmax, but Km increases

24
Q

Noncompetitive inhibition

A

inhibitor binds with equal affinity to enzyme and enzyme-substrate complex. Vmax is decreased Km stays the same

25
Q

Mixed inhibition

A

inhibitor with unequal affinity for enzyme and enzyme substrate complex. Vmax is decreased and Km increases or decreases depending on the inhibitors affinity

26
Q

uncompetitive inhibition

A

inhibitor only binds with enzyme-substrate complex so both Km and vmax decrease

27
Q

zymogens

A

inactive forms of an enzyme that are activated by cleavage

28
Q

Migration velocity

A

v=Ez/f

29
Q

Cadherins

A

calcium dependent glycoproteins hat hold similar cells together

30
Q

integrins

A

have two membrane spanning chains to permit cells to adhere to extracellular proteins

31
Q

selectins

A

allow cells to adhere to carbohydrates on surfaces of other cells. found in the immune system

32
Q

antibody makeup

A

two heavy chains and two light chains held together by disulfide linkages and noncovalent interactions

33
Q

G protein receptor cascade

A

Ligand engages G protein. GDP becomes GTP and the alpha subunit dissociates from beta and lambda subunits. Alpha subunit activates adenyl cyclase or phospholipase C and GTP becomes GDP and alpha subunit reassociates.

34
Q

Equation for number of stereoisomers with common backbone

A

=2^n where n is the number of chiral carbons

35
Q

Benedicts reagent

A

oxidizes glucose to gluconic acid and creates red precipitate to test for the presence of aldehyde

36
Q

Tollens reagent

A

makes a silvery substance when reacted with an aldehyde

37
Q

Esterification of glucose reagents

A

acetic anhydride, 273K, pyridine

38
Q

Phosphorylation of glucose

A

ATP usually occurs with an enzyme

39
Q

maltose

A

(glucose-alpha-1,4-glucose)

40
Q

cellobiose

A

beta 1,4 linkage of two glucose molecule

41
Q

Sucrose

A

(glucose-alpha-1,2-fructose)

42
Q

Lactose

A

(galactose-beta-1,4-glucose)

43
Q

cellulose

A

string of cellubiose (beta 1,4 linkage of two glucose molecule)

44
Q

Amylopectin

A

amylose but also has alpha1,6 bonds

amylose is glucose-alpha-1,4-glucose

45
Q

amylose

A

glucose-alpha-1,4-glucose

46
Q

glycogen

A

highly branched glucose polymer with alpha1,6 bonds more than amylopectin. Highly branched

47
Q

saturated fatty acid

A

has only single bonds (thus saturated with hydrogen)

48
Q

unsaturated fatty acid

A

has some double bonds

49
Q

glycerophosphate

A

As a head group (x) linked to a glycerol backbone via a phosphodiester linkage. Called phosphatidyl-x. examples include phosphatidylcholine and phosphatidylethanolamine

50
Q

sphingolipids

A

have a sphingosine backbone with long chain nonpolar fatty acid tails and polar head groups. Can be phospholipids or glycolipids.

51
Q

Classes of sphingolipids

A

ceramides, sphingomyelin, glycosphingolipids, gangliosides

52
Q

ceramides

A

sphingolipid with Hydrogen as a head group

53
Q

sphingomyelin

A

sphingolipids that are also phospholipids. Usually have phosphatidylcholine or phosphatidylethanolamine as the head group