LCQ #2 BIO101A

storage polysaccharides are…

quick, mobilizable fuel

homopolysaccharide

polymer of only one type of monosaccharide residue

starch, glycogen, cellulose, chitin polymer

heteropolysaccharide

polymer of two or more different monosaccharide residues

Where do amino acids (monomers) differ?

at R group

cellulose

stiff fiber → good for structure

polypeptide have directionality by their

N terminus

C terminus

cholesterol is soluble/insoluble in liquid

insoluble

the sequence of amino acids in a protein

primary structure

protein folding is stabilized by..

H-bonding between =O carbonyl of an AA and

-H on amino end of another AA

Name this structure

B barrel

Name this structure

Alpha helix

Name this structure.

Beta pleated sheet

In global bonding, there is..

H-bonds between _________

Ionic bonds

Covalent bonds— disulfide bridge between

R groups

groups of cysteine

This is isoleucine, is it polar/nonpolar/charged.

Nonpolar.

This is histidine, is it polar/nonpolar/charged.

Charged

This is proline, is it polar/nonpolar/charged.

Nonpolar

This is glutamine, is it polar/nonpolar/charged.

Polar

Quaternary structure

arrangement of polypeptide changes in a protein that has more than one chain

protein function will depend on

conformation

if you see an OH in the R group (amino acid) it is..

Polar

Carbohydrates usually have a

CHO , in a 1:2:1 ratio

Amino acid structure

-NH2 amino group

Carboxylic group

↑ temperature ↑ thermal vibration

overcomes weak H bonds

↓ pH adds hydronium H3O+

disturbs ionic interacitons

neutralizes charge on negatively charged R-group

Fats, oils, steroids, waxes are polymers

False

primary structure

linear sequence of AAs

one end (amino group)

other end (carboxyl group)

N Terminus represents

Amino group

C Terminus represents

Carboxyl Group

Secondary structure

localized area of folding (into a pattern)

alpha helix, beta pleated sheet

Tertiary structure

3-d shape of a protein from side chain interacitions

Nonpolar side groups like water

F

backbone peptide bonds

covalent, within chain

ionic interactions

between charged R groups

disulfide bridges

covalent between cysteine R groups

collagen

several identical polypettides

>2+ polypeptide subunits

native conformation

conformation normally assumed by functional protein

If you heat up a protein →

increases KE, vibration

cause denaturation (vice versa if lowered)