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Leucine and Amino Acid Structures

This document summarizes key concepts about amino acids, peptides, and proteins from Chapter 5 of an organic chemistry textbook. It includes the structure and properties of the amino acid leucine, definitions of isoelectric point and zwitterion, and discusses peptide cleavage by enzymes like trypsin and chymotrypsin. Sample questions assess the reader's understanding of amino acid structures, isoelectric focusing, and peptide fragmentation.

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Amrun Rusrl
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16 views3 pages

Leucine and Amino Acid Structures

This document summarizes key concepts about amino acids, peptides, and proteins from Chapter 5 of an organic chemistry textbook. It includes the structure and properties of the amino acid leucine, definitions of isoelectric point and zwitterion, and discusses peptide cleavage by enzymes like trypsin and chymotrypsin. Sample questions assess the reader's understanding of amino acid structures, isoelectric focusing, and peptide fragmentation.

Uploaded by

Amrun Rusrl
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOC, PDF, TXT or read online on Scribd

Chapter 5 Biomolecules:

Amino Acids, Peptides, and Proteins


Refer to the data below to answer the following questions:
Leucine is an essential amino acid with the systematic name 2-amino-3-methylpentanoic acid. It has pKa1 =
2.36 and pKa2 = 9.60.
1.

Draw the condensed structure for leucine, and label all chirality centers with an asterisk.

2.

How many possible stereoisomers of leucine are there?

4.

What is the pI of leucine?

5.

Draw the structure of the predominant form of leucine at pH 10.00 .

6.

Draw the structure of the predominant form of leucine at pH = 1.50.

8.

Show how leucine might be synthesized using the Knowles enantioselective synthesis.

9.

Show the alkyl halide you would use to prepare leucine by the amidomalonate method.

MATCH a structure from the list below to each of the following terms. Place the letter of the structure in the
blank to the left of the term which it describes.
10.

an octapeptide with a C-terminal valine.

11.

an amino acid in its zwitterionic form.

12.

a polypeptide which gives four fragments on treatment with chymotrypsin.

14.

a carboxyl-protected amino acid.

16.

small organic molecules which act as coenzymes.

50

Chapter 26: Biomolecules: Amino Acids, Peptides, and Proteins

A. [(CH3)3COC ]2 O

B. CH3CHCO
+ NH3

C. Val-Phe-Leu-Met-Tyr-Pro-Gly-Trp-Cys-Glu
O

D. (CH3)2CHCHCOCH2Ph

E. CH3CHCOH

NH2

NH2

F. Asp-Tyr-Ile-His-Pro-Phe-Arg-Val

G. apoenzyme
O

H.

I.

(CH3)3COCNHCHCOH
CH3

Ph

J.

K.

CH3

HO
N

L. Val-Lys-Phe-Gly-Arg-Met-Arg-Phe

M. vitamins

Refer to the data below to answer the following questions:


Amino Acid
Arginine
Glutamic Acid
Tryptophan

Isoelectric point
10.76
3.22
5.89

17. At what pH would you carry out an electrophoresis experiment if you wanted to separate a mixture of
lysine, aspartic acid and phenylalanine? Explain.
18. Define isoelectric point.
19. The most basic amino acid is

20. The most acidic amino acid is ____.

51

Chapter 26: Biomolecules: Amino Acids, Peptides, and Proteins

Refer to the data below to answer the following questions:


Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below.
TyrGlyGlyPheLeuArgArgIleArgProLysLeuLysTrpAspAsnGln
22. What fragments would result if dynorphin were cleaved by trypsin?
23. What fragments would result if dynorphin were cleaved by chymotropsin?

Test Items for McMurrys Organic Chemistry, Seventh Edition

52

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