Ch. 7 Terms (Proteins)

Nutrition

proteins

only macronutrient containing nitrogen and some Sulphur within AA

proteins

the following are all key functions of what?

-structure

-enzymes

-hormones

-transport molecules

-immunity

-blood clotting

-fluid balance

-acid-base buffer

-lubrication

-energy (last resort; 4 kcal/gram)

anatomy of amino acids

amino group, R group, and acid group

r group

only variable part of the amino acid that determines behavior

nonpolar (hydrophobic)

avoid water; fold toward the protein’s core

nonpolar r group examples

leucine, soleucine, valine, alanine, dheylanine

polar (uncharged)

form hydrogen bonds with water; often on protein’s surface

polar r group examples

serine, threonine, asparagine, glutamine, tyrosine

acidic r group (negative)

carry a negative charge; can form ionic bonds with basic side chains

acidic (negatively charged) r group examples

aspartate, glutamate

basic positive r groups

carry a positive charge; histidine is a key pH buffer

basic positive r groups examples

lysine, arginine, histadine

-phenylanine

-valine

-threonine

-tryptophan

-Isoleucine

-methionine

-histidine

-leucine

-lysine

list the 9 essential amino acids (think: PVT TIM HaLL)

-alanine

-aspartic acid

-asparagine

-glutamic acid

-serine

list the nonessential amino acids (think: AAAGS)

-arginine

-cysteine

-glutamine

-glycine

-proline

-tyrosine

list the conditionally essential amino acids: (think: ACGGPT)

gene → transcription → translation → folded protein

sequence order for proteins (determines specific protein)

dipeptide

2 amino acids

tripeptide

3 amino acids

oligopeptide

4-10 amino acids

polypeptide

10+ amino acids

protein

100 + amino acids

primary protein structure

peptide bonds

what are primary protein structures held together by?

secondary protein structure

hydrogen bonds

what are secondary protein structures held together by?

tertiary protein structure

what are tertiary protein structures held together by?

r group interactions

quaternary protein structure

multiple AA chains

-ex: 2 alpha chains and 2 beta chains

what holds quaternary protein structures together

denaturing

unfolding of a protein’s shape, typically by cooking, acid, and agitation

legumes

beans, lentils, peas, soybeans, and peanuts

treenuts

walnuts, cashews, almonds, pecans, and pistachos

amino pattern and digestibility

what are the two key things for protein availability?

carbon skeleton

the remains of an amino acid following removal of the nitrogen-containing component (amino group) of the amino acid

amino acid pool

endogenous source of nitrogen, providing about two-

thirds of the amino acid supply

deaminiation

removing nitrogen, leaving carbon skeleton and ammonia

transamination

transfers amino group to a carbon skeleton

B6

what do deamination and transamination require?

NOT store; only ever used, converted, or excreted

what can the body do with protein?

urea

toxin for removal; can cause liver failure if built up

nitrogen balance

the different states the body can be in, depending on how much nitrogen is taking in, vs put out

0.8→ 1 g protein/kg of bw

protein RDA