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Intramoleculary crosslinked synthetic polypeptides

Intramoleculary crosslinked synthetic polypeptides Intramolecularly Crosslinked Synthetic Polypeptides The study of synthetic polypeptides has yielded many insights into the physical, chemical, and biological behavior of simple polypeptide chains i n solution and has provided a fruitful model system for the more complicated behavior of natural proteins. Up to now, these studies have been concerned primarily with the effects due to variations of the amino acid composition of the polypeptide chains (primary structure) and the organization of the polypeptide chain into the a-helix and the ,&conformation (secondary structure). The studies reported here extend the range of structures available with synthetic polypeptides to intramolecularly crosslinked polymers which promise to provide good model systems for the spatially extended conformations characteristic of the tertiary structure of proteins. The synthetic polypeptide poly G l ~ ~ ~ L y s ~ (No.y3) ' ~ nomen~ T r [for clature, see ref. 1 was intramolecularly crosslinked by two general methods: 1 the use of ionic carbodiimide, l-cyclohexyl-3-(2-morpholinyl-(4)-ethyl)carbodiimide metho-p-toluenesulfonate (iCD) , or Woodward's Reagent K (WRK) to form intramolecular amide bonds between sidechain carboxylic acid and amino groups or the use of 1,5-difluor0-2,4dinitrobenzene (FFDNB) to form 2,4-dinitrophenylene-1,5-bridges between lysine and lysine, lysine and tyrosine, or tyrosine and tyrosine sidechains. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Intramoleculary crosslinked synthetic polypeptides

Biopolymers , Volume 2 (4) – Aug 1, 1964

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Publisher
Wiley
Copyright
Copyright © 1964 John Wiley & Sons, Inc.
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/bip.1964.360020409
Publisher site
See Article on Publisher Site

Abstract

Intramolecularly Crosslinked Synthetic Polypeptides The study of synthetic polypeptides has yielded many insights into the physical, chemical, and biological behavior of simple polypeptide chains i n solution and has provided a fruitful model system for the more complicated behavior of natural proteins. Up to now, these studies have been concerned primarily with the effects due to variations of the amino acid composition of the polypeptide chains (primary structure) and the organization of the polypeptide chain into the a-helix and the ,&conformation (secondary structure). The studies reported here extend the range of structures available with synthetic polypeptides to intramolecularly crosslinked polymers which promise to provide good model systems for the spatially extended conformations characteristic of the tertiary structure of proteins. The synthetic polypeptide poly G l ~ ~ ~ L y s ~ (No.y3) ' ~ nomen~ T r [for clature, see ref. 1 was intramolecularly crosslinked by two general methods: 1 the use of ionic carbodiimide, l-cyclohexyl-3-(2-morpholinyl-(4)-ethyl)carbodiimide metho-p-toluenesulfonate (iCD) , or Woodward's Reagent K (WRK) to form intramolecular amide bonds between sidechain carboxylic acid and amino groups or the use of 1,5-difluor0-2,4dinitrobenzene (FFDNB) to form 2,4-dinitrophenylene-1,5-bridges between lysine and lysine, lysine and tyrosine, or tyrosine and tyrosine sidechains.

Journal

BiopolymersWiley

Published: Aug 1, 1964

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