Biochemistry Flashcards

1
Q

bond length of covalent bond

A

1.54 A and bond every of 85 kcal/mol

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

types of non covalent bonds

A

electrostatic interactions
hydrogen bonds
van der waals interactons

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

Electrostatic Interactions

A

charged group on one molecule attracts an oppositely charged group on another molecule

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

hydrogen bonds

A

electrostatic interactions between two hydrogen molecules

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

van der Waals interactions

A

unequal distribution of electronic charge around an atom fluctuates with time

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

water molecules interact with each other and form strong hydrogen bonds. this property is known as

A

cohesion

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

Hydrophobic effect

A

water, when around a hydrophobic molecule, becomes highly structured and organized

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

hydrophobic forces

A

energy that is measured, formed when water interacts with self, decreasing the energy

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

pKa

A

the pH at which a molecule will lose one of its H+ molecules

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

D or L amino acids are found in proteins

A

L

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

hydrophobic amino acids

A
glycine 
alanine
proline
valine 
leucine
isoleucine  
methionine
phenylalanine 
tryptophan
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

polar amino acids

A
serine 
threonine 
tyrosine
asparagine 
glutamine 
cysteine 
glutamate 
aspartate 
histidine 
arginine 
lysine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Paralogs

A

homologs that form different functions within one species

similar folding patterns/structure

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

Orthologs

A

proteins that form identical or very similar functions in different species

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

4 determinants of folding

A

secondary structure

folding is hierarchical

folding is to some degree context dependent

hydrophobic effect

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

folding is context dependent, this means…

A

many sequences can adopt alternative conformations in different proteins

17
Q

conditions that cause protein denaturation

A

heat
pH (extremes)
Agitation

18
Q

chemicals that cause protein denaturation

A

detergents
chaotrophic agents
organic solvents

19
Q

types of isomers

A

constitutional

steroisomes

20
Q

constitutional isomers

A

differ in the order of attachment of atoms

ex. aldose-ketose pairs

21
Q

types of stereoisomers

A

enantiomers

diastereoisomers

22
Q

stereoisomers

A

same order but different spatial arrangement

23
Q

enantiomers

A

non-superimposable mirror images

ex. D and L glyceraldehyde

24
Q

diastereoisomers

A

isomers that are not mirror images

epimers
anomers

25
Q

epimers

A

differ at one of several asymmetric carbon

d-glucose and d-mannose

26
Q

anomers

A

differ at new asymmetric carbon upon ring closure

ex. alpha-d-glucose, b-d-glucose

27
Q

what binds alcohols and amines

A

glycosidic bonds