Genetics: Analysis and Principles
Genetics: Analysis and Principles
6th Edition
ISBN: 9781259616020
Author: Robert J. Brooker Professor Dr.
Publisher: McGraw-Hill Education
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Chapter 24, Problem 4EQ
Summary Introduction

To review:

The use of tandem mass spectroscopy for determining the sequence of a peptide which in turn, can determine the sequence of the entire protein.

Introduction:

Mass spectrometry (MS) is a technique used for the identification of different proteins by measuring the mass of the peptide fragment. It is most commonly employed for finding out the sequences of proteins. Tandem MS- derived its name as the technique involves two mass spectrometry steps.

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Students have asked these similar questions
Describe the common strategy (steps) for protein sequencing, starting with a biological sample containing many cell and biochemical substances. How prevalent are disulfide links in proteins? Why do the disulfide links need to be broken prior to sequencing? How can they be chemically broken?
Before high performance liquid chromatography (HPLC) methods were devised for the separation and analysis of small peptides, electrophoresis on a paper support was frequently used. Separation was affected on the basis of the charge on a peptide at different pH values. a. Calculate the pI (isoelectric point) of the following primary structures of the following protein i.) Lys- Gly- Ala- Glyii.) Lys- Gly-Ala-Gluiii.) His- Gly- Ala- Gluiv.) Glu- Gly- Ala -Gluv.) Gln-Gly-Ala-Lys b.) the migration toward the cathode, the negative pole; A for the migration toward the anode, the positive pole; and O if the peptide remains stationary.
The sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-K
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