7101 biomolecules, monomers, macromolecules

in what kind of reaction is ATP/NADH/NADPH made?

catabolism because energy is released

in what kind of reaction is ATP/NADH/NAPDH used?

anabolism because energy is required

what are the respective monomers of the following: Proteins, DNA/RNA, Carbohydrates, and biomembranes

amino acids, nucleotides, saccharides, and lipids

what does chiral mean?

optically active (stereoisomers/enantiomers)

what kind of reaction forms monomers into polymers of proteins, DNA, and carbs?

condensation, water released

what does the term amphoteric describe?

a molecule that is acidic and basic

Which isomer is found exclusively in proteins?

the L (levo) isomers

what is the physiological pH?

7.4

a double ionized form of an ion is __________.

zwitteron

what is the isoelectric point?

ph at which positive and negative ions are equal (net ch=0)

what would happen to an amino acid if you raised the pH?

H ion content would lower, deionization of amino acids

what would happen to an amino acid if you lowered the ph?

H ions increase, pronation of amino acids

what does the ionization of a zwitterionic form look like?

one group protonated, one group deprotonated

describe a polar amino acid

water soluble, uneven distribution of e- (polarity)

describe a hydrophilic amino acid

strong affinity for water

describe a non-polar amino acid

non water soluble, even e- distribution (no net chg)

describe a hydrophobic amino acid

lack of affinity for water

describe an amphipathic amino acid

polar and non polar properties

describe an alipatic amino acid

straight or branched chain structure

describe an amphoteric amino acid

can act as an acid or base

what are the neutral amino acids that are sites for sugar linkages?

Serine, Threonine, asparagine (SER, THR, ASN)

What are the polar amino acids?

neutral: SER, THR, ASN,GLN

acidic: ASP, GLU

Basic: HIS, LYS, ARG

what are the amino acids with a negative charge at ph 7?

acidic acids: ASP and GLU

what amino acids have a positive charge at ph 7?

basic amino acids: HIS LYS ARG

which amino acid is associated with disulfide bonds?

cysteine (CYS)

Which nonpolar amino acids can be polarized?

CYS, TYR

what are the nonpolar amino acids?

aliphatic: GLY, ALA, VAL, LEU, ILE

sulfur containing: CYS, MET

aromatic: PHE, TYR, TRP

imino: PRO

what amino acid causes bends in proteins due to its ring shape?

proline

draw out the basic organic functional groups

aldehyde

amide

amino

carbonyl

carboxylic acid

ester

ether

hydroxyl

ketone

methyl

phosphate

sulfhydryl

what does a large Ka value mean for an acid?

stronger acid

what does a small Ka value mean for an acid?

weaker acid

what does a large pKa mean for an acid

weaker acid

what does a small pKa mean for an acid?

stronger acid

during titration, what regions experience the greatest buffering?

when the molecule is either deprotonated or protonated, not during zwitteronic stage

what is the bicarbonate buffer system formula?

CO2 +H2O = H2CO3 = H+ and HCO3-

• it can change ph by H+ ions (higher H+ = lower pH) to create acidic and alkaline environments

• weak acids dissociate into ions

describe a peptide bond.

• a-carboxyl group attached to an a-amino by condensation

• requires energy input

• aka amide bond, very stable

what way does a polypeptide chain run?

N- amino to C- carboxyl terminal

polypeptide chains are a good backbone because they are rich in __________.

hydrogen bonding potential

what is another name for an amino acid unit?

residue

What are enzymes made of (what biological molecule)?

proteins

what are the levels of protein structure?

primary- straight chain (can be connected to other chains by disulfide bonds)

secondary- B sheet and double helix

tertiary- folding and globular

quaternary- combined tertiary structures

what dictated the structure and function of a protien?

amino acid sequence

what are the two categories of proteins, what do they do?

• fibrous- structural

• globular- functional

characteristics and examples of fibrous proteins:

• insoluble in water, unaffected by temp and ph

• collagen, elastin, keratin, and fibrin