Med Chem Part B

Front 1

Primary stucture of protein

Back 1

Simple Chain of amino acids linked by peptide bonds

Front 2

Secondary structure of proteins

Back 2

Consists of regions of ordered structures taken up by the protein chaine

Ie. Alpha helix

Beta pleated sheet

Front 3

Alpha helix

Back 3

Results from coilin of the protein chain, such that the peptide bond making the backbone , form hydrogen bonds these bonds are directed along the axis of the helix, the residues of the helix stick out at right angles from the helix stabilizing the structure.

Front 4

Beta pleated sheet

Back 4

Layering of protein chains, one on top of the other ,here to the structure is held by hydrogen bonds between peptide links

Front 5

Tertiary structure of proteins

Back 5

Overall 3D shape of a protein, obtained by the protein structure folding upon itself,inwich these amino acid residues interact with each other, repulsion and attraction to form a most stable conformation

Front 6

The forces that control the 3D shape of tertiary structure?

Back 6

Covalent

Ionic

Hydrogen

van Der waals

Forces

Front 7

Quatenary structure of proteins

Back 7

Confined to those proteins, which are a combination of a number of protein sub units

Front 8

How do catalysts affect the rate of the rxn without affecting equilibrium

Back 8

They decrease activation energy of a reaction

Front 9

Michaelis constant

Back 9

The substrate [ ] at which the rate of conversion is half of Vmax

Front 10

Vmax in Michael menten eq?

Back 10

Maximum rate of conversion

Front 11

A small Km indicates?

Back 11

Small km= high substrate affinity

Front 12

Substrate witsh smaller km will?

Back 12

Approach vmax more quick

Front 13

The product of catalyst rate constant and the concentration of the enzyme

Back 13

Vmax

Front 14

Ways in which catalysts lower activation energy

Back 14

provide a reaction surface

bring the reactants together

pposition the reactants correctly so that they easily retain there transition state

Catalysts weaken bonds

Catalysts may participate in the mechanism.

Front 15

Active site of an enzyme?

Back 15

Has 3D shape

Has to be near the surface of the enzymes for the substrate to reach it, the site could be a groove, hollow or a tunnel allowing the substrate to sink into the enzyme.

Front 16

Amino acids in the active sites are crucial to the enzymes function, the 2 basic roles of these amino acids are?

Back 16

Binding- The amino acid residue is involved in binding the substrate to the active site

Catalytic- The amino acid is involved in the mechanism of the reaction.

Front 17

The forces which bind a substrate to an active site are?

Back 17

Ionic

Hydrogen

Van Der waals

Front 18

Competitive inhibition

Back 18

Exogenous molecule binds to the active site of the enzyme, blocking access of the endogenous substrate, thus preventing reaction from occuring.

Front 19

Competitive inhibition can be overcome by

Back 19

Increasing level of natural substrate.

Front 20

Non competitive( irreversible) inhibition

Back 20

Binds irreversiblely to the active site of an enzyme, increasing the natural substrate [ ] will not displace inhibitor

Front 21

Non competitive reversible(Alosteric) Inhibitors.

Back 21

Bind to another site of the enzyme(not acive site) causes conformational change, in enzyme action site, so that substrate binding no longer occurs

Front 22

Regulation of enzymes

Back 22

Generally product controls own synthesis by inhibiting the first enzyme in the metabolic pathway, the product binds to the alosteric site and not the active site

Front 23

Enzyme catalyse reactions by providing the following

Back 23

Binding reactions

Acid base catalysis

Nucleophilic group

Front 24

Binding interactions

Back 24

As enzyme changes its shape to maximize bonding interactions, the same thing happens to the substrate, bonds may get stretched and weakend, consequently forcing the substrate into the ideal conformation(transition state) for the reaction to follow

Front 25

Acid/base catalysis

Back 25

Some amino acids in the active site that can serve as proton donors and or acceptors during the catalytic pathway

Front 26

Nucleophilic groups in enzyme catalysis

Back 26

Serine,glutamate, aspartate and cysteine are common inhabitants of active sites, these amino acids have nucleophilic residues OH or SH which are able to participate in the reaction mechanism.

Front 27

Medicinal uses of enzyme inhibitors rationale?

Back 27

If enzyme is responsible for growth, or biochemical pathway responsible for growth, inhibition of such enzyme causes death of the microrganism

Front 28

Oxidorectase function?

Back 28

Enzymes that catalyse oxidation and reduction processes

Front 29

Transferase function

Back 29

Enzymes that catalyse group transfer reactions

Front 30

Hydrolases

Back 30

Enzymes that catalyse hydrolysis reactions

Front 31

Lyases function?

Back 31

Enzymes that catalyse addition/Removal of groups

Front 32

Isomerases function?

Back 32

Enzymes that catalyse isomerization

Front 33

Ligases function?

Back 33

Enzymes that catalyse joining of 2 substrates

Front 34

COX-1 function?

Back 34

Influences the housekeeping function of prostaglandins, which is production of bicarbonate in gastric mucous to prevent gastric tissue damage, maintenance of vascular tissue,nd proper kidney function

Front 35

COX-2 function?

Back 35

Inducible enzyme, involved in inflammatory process, found on few cell types, which include, macrophages and other leukocytes, fibroblasts, and endothelial cells

Front 36

NSAID'S?

Back 36

Non steroidal anti inflammatory drugs, tx of minor pain, and management of edema and tissue damage due to the arthritis, they also posses antipyretic function

Front 37

NSAID'S uses?

Back 37

RA, OA, Acute gouty athritis, ankylosin spondylitis, dysmenohrea and tissue damage from Athritis

Front 38

NSAID'S moa?

Back 38

Inhibit cycloxgenase enzymes

Front 39

COX 1 selective inhibitors?

Back 39

Aspirin, ketoprofen, indomethacin, piroxicam, sulindac

Front 40

Partial COX 2 selective inhibitors?

Back 40

Etodolac,nabumetone, meloxixam

Front 41

Moa of celecoxib and rofecoxib

Back 41

Selective inhibition of Cox-2

Front 42

Antipyretic activity of Nsaids?

Back 42

Result from inhibition of prostaglandins E2 synthesis in the circumventricular organs and near the preoptic hypothalmic area,infections,tissue damage,malignancies etc, enhance the formation of cytokines that increase PGE2, triggers the hypothalamus to promote increase in heat generation and decrease in heat loss