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Derivation of the small‐angle x‐ray scattering functions for local conformations of polypeptide chains in solution
Author(s) -
Muroga Yoshio
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(20011015)59:5<320::aid-bip1029>3.0.co;2-#
Subject(s) - chemistry , small angle x ray scattering , scattering , crystallography , small angle scattering , x ray , wide angle x ray scattering , chain (unit) , polypeptide chain , optics , small angle neutron scattering , physics , quantum mechanics , biochemistry , neutron scattering , amino acid
The small‐angle x‐ray scattering (SAXS) functions are analytically derived for both the randomly coiled and helical local conformations of a polypeptide chain in solution. The resulting scattering functions for helices of various types are characterized by a maximum in the range of scattering‐vector corresponding to Bragg spacings of 3–5 Å, whereas the random‐coil function has no maximum. This result is compatible with the extant SAXS data for partially neutralized poly( L ‐glutamic acid) and poly( L ‐lysine) in aqueous solutions. Comparison of the SAXS data with the calculated scattering functions shows that helical structures in both polypeptide chains are of the 3.6 13 ‐helix (α‐helix) rather than 3.0 10 ‐type. © 2001 John Wiley & Sons, Inc. Biopolymers 59: 320–329, 2001