Biochem Exam 1

Front 1

Common chemical groups

Back 1

C-O Bond: Alcohol, aldehydes, ketones, carboxylic acid, ehter, acid anhydride.
C-S: Suflhydryl, disulfide.
C-N: amino, quaternary amine
Ester and amides: ester, thioester, phosester, amide

Front 2

Five common reactions

Back 2

condensation, redox, cleavage, rearrangement, group transfer

Front 3

enantiomer

Back 3

sterioisomers that ar emirror images of each other

Front 4

diastereomers

Back 4

isomers that have opposite configurations at one or more chiral center but are not mirror images of each other.

Front 5

epimers

Back 5

molecules that differ at only one chiral carbon.

Front 6

essential amino acids

Back 6

leucine, isoleucine, lysine, valine, phenylalanin, tryptophan, threonine, methionine, histidine, arginine

Front 7

hydrogen bonds

Back 7

electronegative forces from atom such as oxygen to electopositive forces of hydrogen.

Front 8

ionic bonds

Back 8

bonds between formal negative and formal pos charged atoms.

Front 9

van der waals

Back 9

induced electopositive force produced on one atom as it approaches another atom

Front 10

hydrophobic interactions

Back 10

force producee when nonsoluble molecules are in polar solutions. water has reduced entropy when it can surround large molecules rather than smaller molecules.

Front 11

cyclic form of aldose

Back 11

pyranose (5 carbons)

Front 12

cyclic form of ketose

Back 12

furanose (4 carbons)

Front 13

glycosaminoglycans

Back 13

long chain of repeating amino sugar dissacharides. Lots of negative.

Front 14

what is not able to be a reducing sugar ever?

Back 14

ketose

Front 15

amino acid without a chiral carbon

Back 15

glycine

Front 16

essential amino acids

Back 16

histidine, methionine, threonine, phenolalanine, isoleucine, leucine, lysine, valine, arganine, tryptophans

Front 17

important amino acids not found in proteins

Back 17

creatine, carnitine, taurine, etc..

Front 18

when pH>pKa

Back 18

will deprotonate

Front 19

pH<pKa

Back 19

protonates

Front 20

four weak forces

Back 20

hydrogen bonds, ionic, hydrophobic, van der waals

Front 21

α H chain

Back 21

IgA: first line of defense. In saliva, tear ducts, etc..
-all are based on C region of H chains

Front 22

γ H chain

Back 22

IgG: Passed mother to child. Found in blood.

Front 23

μ H chain

Back 23

IgM: first antibody to appear in an immune response

Front 24

ε H chain

Back 24

IgE: mediates allergic reactions

Front 25

Collagen

Back 25

three collagen proteins form triple helix (proline, 4-hydroxyproline, lysine). Stabilized with H-bonds

Front 26

fibrils

Back 26

ordered arrays of collagen triple helices. Stabilized by covalent bonding. Crosslinks b/w them dependent on Vitamin C

Front 27

ligase

Back 27

join molecules with condensation

Front 28

lyases

Back 28

split molecules with water byproduct.

Front 29

serine proteases

Back 29

splits protein in to smaller polypeptides. Specificity determined by binding pocket. ex: chymotrypsin and trypsin

Front 30

michaelis-menton equation

Back 30

V=Vmax[S]/Km+[S], Km is inversely proportional to affinity.

Front 31

hexokinase and glucokinase

Back 31

hexo: found in most cells, gluco: found only in liver
glucose low in most cells, high in liver, therefore hexo has high affinity and gluco does not

Front 32

lineweaver-burke

Back 32

1/V= Km/Vmax(1/[S])+ 1/Vmax
X int: -1/Km

Front 33

types of cofactors

Back 33

coenzymes and essential ions

Front 34

types of essential ions

Back 34

activator ions (loose) and metal ions of metalloenzymes(tight)

Front 35

types of coenzymes

Back 35

cosubstrates(loose) and prosthetic groups(tight)

Front 36

niacin is vitamin source for what?

Back 36

NAD and coenzyme A-oxidation/reduction and transfer of acyl groups

Front 37

Riboflavin B2 is source for what?

Back 37

FAD and FMN-oxidation reduction

Front 38

Vitamin B1 for what?

Back 38

TPP-transfer of two carbon fragments contain carboxyl group (used in synthesis of acetylcholine)

Front 39

nicotinamide coenzymes

Back 39

used in reactions involving hydride ion

Front 40

NAD+/NADH

Back 40

acts like a true cosubstrate: binds like substrate and exits like product

Front 41

biotin

Back 41

very important for metabolism. used as is

Front 42

Vitamin B6

Back 42

PLP-carries out reactions with amino acids

Front 43

lipoamide

Back 43

formed from lipoic acid. similar to coenzyme a-acyl group carrier. also has redox properties

Front 44

lipid soluble vitamins

Back 44

A,K,D,E

Front 45

Heme

Back 45

Example of prosthetic group. Also biotin and lipoamide.

Front 46

four types of lipids

Back 46

fatty acids,and isoprenoids (steroids, lipid vitamins and terpenes)

Front 47

two of the four types of fatty acids we studied

Back 47

sphingolipids and triacylglycerides

Front 48

types of sphingolipids

Back 48

ceremides-> sphingomyelins, cerebrosides

Front 49

Saturated fatty acids, carbons 12,14,16,18,20

Back 49

lauric acid, myeristic acid, palmitic acid, stearic acid, arachidic acid

Front 50

unsaturated fatty acids, 20 carbonds

Back 50

arachidonic acid, has four double bonds-key fatty acid in signaling and synthesis of key biomolecules-made from linoleic or linolic acid b/c can't be made de novo.

Front 51

triacylglycerols

Back 51

very hydrophobic. Storage mechanism for fatty acids. fatty acids cleaved by lipases.

Front 52

glycerophospholipds

Back 52

similar to triacylglycerols except third carbon has phosphate moiety.

Front 53

glycerophospholipid head groups (5)

Back 53

phosphatidylethanolamines, phosphatidylserines, phosphatidylcholines,phosphatidylinositols, and other phosphatidylglycerol

Front 54

cerebroside, gangliosides

Back 54

sphingolipids with single sugar or polysacharide attached.

Front 55

what controls ABO bloodtyping?

Back 55

glycolipids and glycoproteins

Front 56

what is the glycocalyx

Back 56

network of glycoproteins and proteoglycans that extend outward from the cell.

Front 57

mammalian cells that have glycocalyx

Back 57

platelets, endothelial cells, sperm, fertilized ovum, and cancer cells

Front 58

what are glycosaminoglycans

Back 58

mixed monosaccharides with repeating disaccharide units. one of the mono. is always an amino sugar.

Front 59

four classes of GAGs

Back 59

hyaluronic acid, condroitin sulfates, heparin, keratin sulfates

Front 60

what is a proteoglycan

Back 60

GAG attached to a protein core. bottle brush structure. lots of neg charge leads to long structure.

Front 61

what residue is involved in n-linked glycoprotein

Back 61

asparagine

Front 62

which residues are in o-linked glycoproteins

Back 62

serine, threonine and hydroxylysine

Front 63

vant hoff's law

Back 63

pi=CRT (osmotic pressure directly prop. to concentration of osmotically active particles)

Front 64

osmolality

Back 64

osmoles/kg

Front 65

osmolarity

Back 65

osmoles/liter

Front 66

primary components of serum osmolarity

Back 66

glucose, Na, HCO3-, Cl and urea