Biochem

Question 1

Understand the polypeptide bond

Answer 1

repetitive peptide bonds allow for the formation of receptive H bonds and the formation fo the secondary structures

Question 2

two type of secondary protient structures

Answer 2

alpha helix and beta sheets

Question 3

Teritary structures

Answer 3

can have both alpha and beta structures

Question 4

Quaternary structures

Answer 4

When two or more poly peptides form together

Question 5

Prosthetic group

Answer 5

a non portion component found of some protiens

Mb and Hb

Question 6

Allosteric regulation for Hb

Answer 6

allosteric meaning other side which is where Hb can attach

Question 7

A porphyrin ring

Answer 7

has 4 cyclic ring structures

Question 8

Heme is a ____ w/ a ____ center

Answer 8

porphyrin ring q and a ferrous ion

Question 9

Hemoglobin(Hb) ____ RBCs

Answer 9

transports O2

Question 10

Myoglobin(Mb) ___ O2

Answer 10

Storage in the muscles

Question 11

Proximal histamine

Answer 11

When Heme is w/o O2 then there proximal histamine is attached to Fe

Question 12

Distal histidine

Answer 12

When the 02 attached to a heme and then attached to another heme

Question 13

How many bonds can Fe2+ form

Answer 13

6 covalent bonds

Question 14

How does Fe2+ protected

Answer 14

It is embedded deep w/ in the porphyrin ring and deep in the global protein

Question 15

Myoglobin has what type of dissociation curve

Answer 15

hyperbolic

Question 16

Hemoglobin is a ____ if __ polypeptide chains

Answer 16

tetramer and 4

Question 17

HbA is a pair of identical ___

Answer 17

ab dimmers

Question 18

4 globin monomers means that ___ O2 molecules can be carried on Hb

Answer 18

4

Question 19

When Hb is “T” or Taut then the the molecule is

Answer 19

deoxygenated

Question 20

when the Hb is “R” and relaxed the structure is oxyhemoglobin

Question 21

Why is histidine used

Answer 21

It helps buffer the pH of the blood as well as regulate the O2 affinity

Question 22

When O2 binds to heme ring the ring assumes more of a ___ shape

Answer 22

planer. this tugs on the proximal histidine amino acid which tugs on a-helix and changes shape to a globin monomer

Question 23

What is cooperative ligand binding in association to heme

Answer 23

When one O2 binds then the affinity for O2 increases causing all 4 locations to become oxygenated

Question 24

Why is O2 a positive allosteric

Answer 24

because binding of 02 at once site increase affinity for o2 at other sites

Question 25

What type of curve is cooperative binding?

Answer 25

sigmoidal

Question 26

Can Co2 react w/ amino terminus of a-chain

Answer 26

yes by creating a carbamate structure an | but it does not bind to FE in heme it just binds acts a carrier

Question 27

What effects do 2,3 BPG have on Hb o2 affinity

Answer 27

it decreases it when levels are high and causes o2 to release

Question 28

pH is the

Answer 28

-log[H+]

Question 29

Kw is defined as the

Answer 29

equilibria constant

Question 30

Kw=[H+][Oh]=10^-14

Question 31

Ka+ equilibrium constant

Answer 31

pKa=-logKa

Question 32

Strong Acids have a ___ Ka and a ____ pKa

Answer 32

Large and small

Question 33

Buffer area is where the __ is unchanged

Answer 33

pKA

Question 34

Henderson hasselbalch eq

Answer 34

pH=pKA+log([HA]/[A])

Question 35

Urea

Answer 35

Question 36

Transanimation reaction

Answer 36

removing Nh3 fr

Question 37

A-keto Acid a-amino acids

Answer 37

Aminotransferase

Question 38

Transport NH3 from most tissues is

Answer 38

Glutamine

Question 39

Urea cycle

Answer 39

Understand map out