Proteins & enzymes

Question 1

What protein structure(s) are lost during denaturation?

Answer 1

secondary and tertiary

rarely in primary

Question 2

what is post or co-translational modification of a tertiary structure?

Answer 2

when the protein becomes a Quaternary structure (adding molecules to the protein)

Question 3

what are gylcoproteins ,lipoproteins and metalloproteins? and what group of proteins are they examples of

Answer 3

1. carbohydrates combined with proteins
   2.lipids combined with proteins
2. metal ions in a protein

All conjugated proteins

Question 4

what is another name for a protein that has a Quaternary structure ?

Answer 4

conjugated proteins

Question 5

what is protein Glycosylation?

Answer 5

when a carbohydrate is attached to a protein and undergoes post or co-translational modification to create a glycoprotein

Question 6

what are the effects of protein glycosylation ?(4)

Answer 6

-stability
-solubility
-orientation
-cell signalling

Question 7

role of lipoproteins ?

Answer 7

transport hydrophobic lipids

Question 8

What is the complexes called that a group of lipoproteins can form?

Answer 8

apolipoproteins

Question 9

what is the role of apolipoproteins ?

Answer 9

transport lipids in blood and cerespinal fluid

Question 10

give an example of a metalloprotein

Answer 10

haemoglobin

Question 11

what ion does haemoglobin contain?

Answer 11

iron

Question 12

What amino acid changes in a sickle cell infected cell?

Answer 12

glutamate becomes Valine

Question 13

where do you find fibrous protein?

Answer 13

bone, connective tissue ,collagen

Question 14

role of globular & give examples

Answer 14

transport,hormones,enzymes etc

e.g haemoglobin

Question 15

What causes high levels of cholesterol in hypercholesterolemia

Answer 15

(things to do with errors in receptors & receptor not release LDL i.i low density lipoproetein

Question 15

how are biological catalyst different from chemical ones?

Answer 15

catalyse high reaction rates etc

Question 16

What is a cofactor?

Answer 16

nonprotein chemical/metalic ion that is seen as a helper molecule (helps cataylse things)

Question 17

what are isoenzymes

Answer 17

enzymes that catalyse the same reaction but have different structure etc

Question 18

how can enzymes be used in a clinical setting?

Answer 18

1.detect tissue damage & origin of the affected tissue
2. notice how diseases relates to enzyme problems

Question 18

what do ezymes do to the activation energy?

Answer 18

lowers it , so cataylsedreactions have lower AE than an un-catalysed one

Question 19

lipoproteins, metaloproteins and glyocoproteins are all examples of what group of proteins?

Answer 19

conjugated proteins

Question 20

what is the name of the graphical plot for analysis of Michaelis-Menten equation?

Answer 20

Line-weaver burk plot

Question 21

what is competitve inhibition?

Answer 21

an inhibitor competes with the SUBSTRATE for binding to the active site

Question 22

what effect does competitive inhibition have on Vmax and Km?

Answer 22

Vmax unchanged
Km increases as will take longer to overcome inhibiton

Question 23

what is a non-competitive inhibition?

Answer 23

an inhibitor that binds to an allosteric site, altering the shape of the active site

Question 24

what effect does non-competitive inhibiton have on vmax and km?

Answer 24

vmax decreases km remains the same

Question 25

specific enzymes are specifc to one tissue , true or false?

Answer 25

false- specific enzymes can be found in varies tissues

Question 26

what analysis technique is used to determine the type of enzyme

Answer 26

electrophoresis

Question 27

what disease is linked to alpha galactosidase ?

Answer 27

fabry disease

Question 28

what do cholinesterase aid function of ?

Answer 28

central nervous sysetm

Question 29

what are 3 types of protein

Answer 29

globular : funnction, storage, enzymes, hormones, transporters, structural membranous fibrous

Question 30

give an example of a globular protein

Answer 30

immunoglobulin

Question 31

define primry structure

Answer 31

sequence of amino acids creating polypeptide chain

Question 32

what type of reaction is a peptide bond holding amino acids together called?

Answer 32

dehydration reaction

Question 33

define secondary structure

Answer 33

hydrogen bond interactions within the protein to give 3D structure

Question 34

define tertiary structure

Answer 34

functional groups of R chains interact with each other

Question 35

define quaternary structure

Answer 35

2 or more polypeptides interact