Sequence analysis of polypeptides via terminal n-thiobenzoyl derivatives
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Sequence analysis of polypeptides via terminal n-thiobenzoyl derivatives

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Published by Oxford Polytechnic in Oxford .
Written in English


Book details:

Edition Notes

Thesis (Ph.D.) - Oxford Polytechnic, Oxford, 1973.

StatementJohn Hume.
ContributionsOxford Polytechnic. Department of Science.
The Physical Object
Pagination(vi),166p. ;
Number of Pages166
ID Numbers
Open LibraryOL18542884M

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The N-terminal sequence of CP29 is subject to a series of processing events: excision of Met1, acetylation of Val2, and phosphorylation of Thr7 (Turkina et al., ). These alterations could be the reason why the transit peptides are retained (Turkina et al., ). Synthesis of polypeptides via bioinspired polymerization of in situ purified N -carboxyanhydrides Article (PDF Available) in Proceedings of the National Academy of Sciences (22)   The base peptide sequence LRFKY-NH 2 (2) by itself, which has an N-terminal Leu and a Lys with an ε-amino side-chain, was practically resistant to N-terminal   at the N-terminal end of the polypeptide chain, to form a phenylthiocarbamyl derivative of the terminal residue. Basic conditions are required for this reaction. Edman originally used pyridine to generate a pH of Alternatives used since include ‘Quadrol’, trimethylamine and N-methylpiperidine. Clearly, a free a-amino group

About this book Introduction This edition includes not only novel approaches to the validation of quality assurance methods, reflecting the current importance of biopharmaceuticals, but also offers a guide to the analysis of protein sequence information via the powerful new tools of ://   Protein sequencing is the practical process of determining the amino acid sequence of all or part of a protein or may serve to identify the protein or characterize its post-translational lly, partial sequencing of a protein provides sufficient information (one or more sequence tags) to identify it with reference to databases of protein sequences derived from coupling of the C-terminal amino acid to the solid matrix. The Nα (A) group is then removed by treatment with trifluoroacetic acid (TFA) in the t-Boc strategy and with piperidine in the Fmoc strategy. The next (Nα protected) amino acid is coupled to the already synthesized peptide chain bound to the polymeric matrix and, once coupled, ?ej The protein of interest having been purified and its mass determined, the next analysis usually performed is to determine the protein's amino acid sequence, or primary structure. As stated previously (Section ), a wealth of information about a protein's function and evolutionary history can often be obtained from the primary structure. Let us examine first how we can sequence a simple

Polypeptides and proteins can be used to cleave sequentially the N-terminal residue of a peptide without the need for total hydrolysis. which also suppresses racemization via the oxazalone. N C NR R R1 O O H N O N H R R O R1 H2N R2 O R1 N R2 N H O N H RR H N R O N H R O R1 R1 O N O NNHO N N N ureaN-acylurea O-acylisourea HOBt HOBt Analysis of the primary structure of a peptide is, in fact, elucidation of its amino acids sequence using chromatography which can be achieved employing simple amino acid analysis, in conjunction with sequencing methods such as N-terminal residue identification by Edman degradation, or peptide mapping coupled with mass spectrometry (Heinrikson This book is an update to the much-acclaimed first edition with new and updated techniques for determining the sequence of proteins and peptides. This edition includes not only novel approaches to the validation of quality assurance methods, reflecting the current importance of biopharmaceuticals, but also offers a guide to analysis of protein 1. Which one of the following statements about beta-gamma methylene and beta-gamma imino derivatives of purine and pyrimidine triphosphates is CORRECT? A. They are potential anticancer drugs B. They are precursors of B vitamins. C. They readily undergo hydrolytic removal of the terminal