Lec 4&5

Question 1

If the primary structure of the normal and mutated proteins are known, this information may be used to what?

Answer 1

used to diagnose or clinical study of the disease.

Question 2

Protein misfolding diseases example

Answer 2

Mad Cow Disease, Alzheimer’s, Parkinson’s Disease, and Creutzfeldt-Jakob disease.

Question 3

Causes of sickle cell anemia Replacing valine with glutamic acid? T/F

Answer 3

F, replacing glutamic acid with valine

Question 4

Example of treatment that cause a protein to unfold

Answer 4

heat, pH changes, detergents, urea.

Question 5

all amino acids are Beta-amino acids.
T/F?

Answer 5

F, are α-amino acids.

Question 6

is the further folding of the polypeptide stabilized by interactions between R groups .

Answer 6

tertiary structure

Question 7

tertiary structure It is formed when alpha-helices and beta-sheets are held together by?

Answer 7

weak interactions.

Question 8

quaternary structure exists in proteins with?
A. more than one polypeptide chain
B. One polypeptide chain

Answer 8

A. more than one polypeptide chain

Question 9

protein that usually does not fold independently of the rest of
the protein

Answer 9

motif

Question 10

PDB can be searched by?

Answer 10

• typing the description
• partial sequence
• PDB ID

Question 11

involved in apoptotic signal transduction.

Answer 11

death domain

Question 12

assembly of protein complexes on chromatin; 30-70 amino acids

Answer 12

Chromo

Question 13

50 amino acids and involved in protein-protein interactions

Answer 13

SH3 (Srchomology 3) domain

Question 14

using techniques like X-ray crystallography, (NMR) spectroscopy, and cryoelectron microscopy.

Answer 14

PDB

Question 15

All proteins functions are undependent on their structure
T/F?

Answer 15

F, dependent

Question 16

(the normal isoform of PrP protein) with prominent α-helices

Answer 16

PrPC for Creutzfeldt–Jacob disease

Question 17

(the abnormal isoform) with prominent βsheets.

Answer 17

PrPsc

Question 18

Inherited mutations in the Prion protein (PrP)

Answer 18

Creutzfeldt–Jacob disease

Question 19

all amino acids are?

Answer 19

α-amino acids.

Question 20

secondary structure of the protein is the formation of α-helixes and β-pleated sheets stabilized by ….?

Answer 20

by hydrogen bonding

Question 21

folding is a result of hydrogen bonding between the amine and carboxyl groups of adjacent amino acids.
T/F?

Answer 21

F, non-adjacent amino acids

Question 22

with more than one polypeptide chain and held together by a variety
of bonds (similar to tertiary structure).
Which type of structure?

Answer 22

quaternary structure