BIO 002 - Midterm 1

Amide

Draw, p/d state if it has, state properties

polar

Carboxylic Acid

Draw, p/d state if it has, state properties

can be protonated or deprotonated

acidic

Amine

Draw, p/d state if it has, state properties

can be protonated or deprotonated

basic

Phosphate

Draw, p/d state if it has, state properties

can be protonated/deprotonated

polar

methyl

Draw, p/d state if it has, state properties

nonpolar

thiol

Draw, p/d state if it has, state properties

polar

thioester

Draw, p/d state if it has, state properties

polar

hydroxyl

Draw, p/d state if it has, state properties

polar

draw an amino acid

circle backbone

What is pH?

numerical measurement of hydrogen ions concentration within a solution on a negative logarithm

Hydrolysis

Water added to polypeptide chain, breaks the peptide bond

Define primary structure

• draw

linked by peptide bonds( or amides), basic linear arrangement, is non functional

define secondary structure

• draw

held together by hydrogen bonds b/w backbone atoms, folds into alpha helixes or beta pleated sheets

define tertiary structure

• draw

the 3D shape of a protein held together by many electrostatic interactions b/w the R-groups of an AA. is a functional protein

define quaternary structure

• draw

multiple different protein subunits held together by the same interactions as tertiary structures, but interactions happen b/w the R-groups of the tertiary structure subunit proteins

enzyme

catalyzes rxns by binding reactants and lowering the activation energy of the rxn

allosteric enzymes

enzymes that can be up/down regulated, have an allosteric site

allosteric site

place where an allosteric molecule (activator/inhibitor) binds and changes the shape of the enzyme’s active site

What are the EN and EP elements?

How do we find the nonpolar covalent bonds or polar covalent bonds?

EN → higher EN #

• O, N, S

EP → lower EN #

• C, H, P

Nonpolar covalent bond: EN-EN or EP-EP

Polar covalent bond: EN and EP

How to find carbohydrates

• have C, H, O (fixed ration 1:2:1)

• have OH groups

• can be ring or linear

Monosaccarides

simple sugars

• 3-7 bonds

• very soluble

Disaccharides

two monosaccharides combined via a dehydration/condensation reaction

• forms glycosidic bonds/linkages

• broken via hydrolysis

how to find nucleic acids

• has a nitrogenous base (ring like structure with nitrogen), a pentose sugar and a phosphate group

How to find lipids

• contain many C-H bonds, no fixed ratio

• more carbons than oxygen

• has long chains of C-H bond

How to find proteins

• Have C, H, N, O

• have animo and carboxylic groups

• can be protonated/deprotonated

• have N-C-C backbone (or C-C-N)

N-terminus

• Start of polypeptide

• the free amino group (NH₂/NH₃)

C-Terminus

• End of polypeptide

• free carboxyl group (-COOH)

condensation reaction

• draw it

water removed from two amino acids coming together, forming a peptide bond (and new amide functional group)

hydrolysis

• draw it

water added to polypeptide chain, breaks the peptide bond

hydrophobic

water fearing

• nonpolar compounds

hydrophillic

water loving

• polar/charged compounds

phospolipids

polar “head” and nonpolar “tail”

saturated

• carbons are “saturated” with hydrogens

unsaturated

the carbons are lacking hydrogens

• lead to kinks in the tail

What are the two kinds of transport?

• Passive transport: transport of a molecule doesnt require energy goes down or with concentration gradient

• Active transport: moves compounds against the concentration gradient, requires energy

  • energy comes from ATP hydrolysis or through passive transport of another molecule

What are the two diffusions in passive transport?

• passive diffusion

  • doesnt need a channel protein

• facilitated diffusion