Log in
Chemistry
1
answer
0
watching
89
views
12 Dec 2019

what peptide fragments would be generated by cleavage of the following peptide with chymotrypsin? GIVEQCCHKRCSEYNLQNYCN

Watch
1
answer
0
watching
89
views

For unlimited access to Homework Help, a Homework+ subscription is required.

Sixta Kovacek
Sixta KovacekLv2
13 Dec 2019

Unlock all answers

Get 1 free homework help answer.
Already have an account? Log in
Share
discord banner image
Join us on Discord
Chemistry Study Group
Join now

Related textbook solutions

Basic Chemistry
5 Edition,
Timberlake
ISBN: 9780134138046
Principles of Chemistry Molecular Approach
4th Edition,
Tro
ISBN: 9780134112831
Principles of Chemistry Molecular Approach
3rd Edition, 2014
Tro
ISBN: 9780321971944
Chemistry: Structure and Properties
2nd Edition,
Tro
ISBN: 9780134293936
Chemistry: A Molecular Approach
3rd Edition,
Tro
ISBN: 9780321809247
Chemistry: A Molecular Approach
5th Edition,
Tro
ISBN: 9780134874371
Principles of Chemistry: A Molecular Approach
4th Edition,
Tro
ISBN: 9780134895741
Chemistry: The Central Science
14th Edition, 2017
Brown
ISBN: 9780134414232

Related questions

A mutant form of peptide hormone angiotensin II has the amino acid composition Asp,
Arg, Ile, Met, Phe, Pro, Tyr, Val. The following observations are made:
• Trypsin yields a peptide containing Asp and Arg, and a hexapeptide with all the
rest. Trypin cleaves on the C-side of Lys and Arg.
• Cyanogen bromide (CNBr) cleavage yiealds a dipeptide containing Phe and Pro,
and a hexapeptide containing all others. CNBr cleaves on the C-side of Met.
• Chymotrypsin cleaves into two tetrapeptides, of composition Asp, Arg, Tyr, Val and
Ile, Met, Phe, Pro. Chymotrypsin cleaves on the C-side of Tyr, Trp, and Phe.
• The dipeptide of composition Pro, Phe cannot be cleaved by chymotrypsin
The sequence of the peptide is:

(PLEASE EXPLAIN THE ANSWER)

The following reagents are often used in protein chemistry: CNBr, Urea, Mercaptoethanol, Chymotrypsin, Trypsin, Performic acid, 6 N HCl, and Phenyl isothiocyanate. Which one is the best suited for accomplishing each of the following tasks?

a) Determination of the amino acid sequence of a small peptide.

b) Reversible denaturation of a protein devoid of disulfide bonds. Which additional reagent would you need if disulfide bonds were present?

c) Hydrolysis of peptide bonds on the carboxyl side of aromatic residues.

d) Cleavage of peptide bonds on the carboxyl side of methionines.

e) Hydrolysis of peptide bonds on the carboxyl side of lysine and arginine residues.

Weekly leaderboard

Home
Homework Help 3,900,000
Chemistry 830,000
Start filling in the gaps now
Log in