Term
|
Definition
| compete for H bonds which are involved in maintaining higher levels of protein structure |
|
|
Term
| Acid and Base denaturants |
|
Definition
ACID- protonate carboxylate functions which removes their charge; destroy salt bridges
BASE- deprotonate ammonium which removes charge; destroys salt bridges |
|
|
Term
|
Definition
| competes for H bonds which are responsible for maintaining higher levels of protein structure |
|
|
Term
|
Definition
| increases thermal motions which disrupt noncovalent interactions |
|
|
Term
|
Definition
| bond to free thiol function (-S-H) and cause protein to precipitate |
|
|
Term
|
Definition
most are made from b-vitamins
loosely or tightly bound to enzyme
tightly bound coenzymes are considered to be prosthetic groups |
|
|
Term
|
Definition
coenzyme required by most but not all dehydrogenases
remove hydrogen from substrate
binds a hydride ion to become NADH |
|
|
Term
|
Definition
| a single polypeptide chain |
|
|
Term
|
Definition
| nonprotein molecule that a protein require for activity |
|
|
Term
| prosthetic group of myglobin |
|
Definition
| heme, an iron 2+ ion ( Fe 2+ coordinated to a poryphorin ring) |
|
|
Term
| why doesn't myoglobin have quaternary structure? |
|
Definition
| it is a monomeric protein so it doesnt have interactions between chains |
|
|
Term
| hemoglbin/myoglobin similar/different |
|
Definition
both are oxygen carriers
both use heme as a prosthetic group
myoglobin is monomeric
hemoglobin is tetrameric |
|
|
Term
| why does hemoglobin have quaternary structure while myglobin does not |
|
Definition
| because hemoglobin is tetrameric so multiple chains can interact while myoglbin is monomeric so it doesnt have multiple chains |
|
|
Term
|
Definition
| an optical isomer that is non-suoerimposable on its mirror in=mage |
|
|
Term
|
Definition
| an optically inactive mixture that consists of equal amounts of a pair of enantiomers |
|
|
Term
|
Definition
| structures that belong to the same family of optical isomers but are related as enantiomers |
|
|
Term
|
Definition
| an optical isomer that rotates the plane of light to the right |
|
|
Term
|
Definition
| an optical isomer that rotates the plane of light to the left |
|
|
Term
|
Definition
| a substance able to rotate the plane of light |
|
|
Term
| how do A.A. residues which are typically far apart in promary structure get close to each other to form the active site? |
|
Definition
| the protein must fold properly |
|
|
Term
|
Definition
| class of enzymes that catalyzes the removing of hydrogen from substrates in catabolic pathways like glycolysis and Krebs Cycle |
|
|
Term
|
Definition
| most dehydrogenases must use this and are NAD+ dependent |
|
|
Term
|
Definition
| some dehydrogenases use this as the electron/proton carrier and are therefore FAD dependent |
|
|
Term
| carbs digest ----> glucose, sugars/glycolysis ----> pyruvate ----> acetyl CoA/citric acid cycle----->reduced coenzymes/ETC ---> ATP |
|
Definition
|
|
Term
| places where products of A.A. can join central metabolism pathway |
|
Definition
| acetyl CoA, pyruvate, citric acid cycle intermediates |
|
|
