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Further characterization of the kinetic folding intermediate of αα‐tropomyosin and of its 142–281 subsequence
Author(s) -
Mo Jianming,
Holtzer Marilyn Emerson,
Holtzer Alfred
Publication year - 1993
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/bip.360330510
Subject(s) - chemistry , folding (dsp implementation) , tropomyosin , subsequence , tyrosine , crystallography , kinetic energy , helix (gastropod) , myosin , biochemistry , mathematical analysis , ecology , quantum mechanics , snail , electrical engineering , bounded function , biology , engineering , physics , mathematics
The backbone CD spectrum from 250 to 212 nm for the kinetic folding intermediate of αα‐tropomyosin (αα‐Tm) and nonpolymerizable αα‐Tm was obtained. The spectrum shows that the intermediate is indeed α‐helical with about 70% of the equilibrium α‐helix content. Subsequence 142 Tm 281 of the α‐tropomyosin chain has five tyrosine residues (at positions 162, 214, 221, 261, 267). Stopped flow CD at the negative peak in the tyrosine spectral region (280 nm) shows that any tyrosine residues that contribute to the spectrum in the region have already reached their final state in the fast phase of folding ( < 0.04 s). © 1993 John Wiley & Sons, Inc.