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Use of sequence‐specific tri‐block copolymers to determine the helix‐forming tendencies of amino acids
Author(s) -
Rothwarf David M.,
Davenport V. Gary,
Shi PuTau,
Peng JinLin,
Scheraga Harold A.
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199610)39:4<531::aid-bip5>3.0.co;2-y
Subject(s) - copolymer , chemistry , helix (gastropod) , block structure , block (permutation group theory) , residue (chemistry) , amino acid , peptide , sequence (biology) , polar , crystallography , stereochemistry , polymer chemistry , biochemistry , polymer , organic chemistry , thermodynamics , physics , combinatorics , ecology , mathematics , astronomy , finite element method , snail , biology
In order to examine the helix‐coil transition of water‐insoluble polypeptides, without requiring interspersion of charged or polar residues within the sequence, a tri‐block copolymer strategy has been developed to determine the helix propensity of amino acids in short (15‐residue) peptides. The method is also well suited to evaluate specific interactions that contribute to helix formation. In this approach, measurement is made of the helix content of the central block of tri‐block copolymers of the type Lys 15 ‐X‐Lys 15 , where X is the 15‐residue peptide whose helix content is being investigated. The suitability of tri‐block copolymers of this type has been verified experimentally by using the water‐soluble peptide (Ala 2 GlnAla 2 ) 3 as the central block. The CD spectrum of the central block in the tri‐block copolymer and of Ac‐(Ala 2 GlnAla 2 ) 3 ‐NH 2 are indistinguishable within experimental error. © 1996 John Wiley & Sons, Inc.