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A 13C-NMR study on the conformational and dynamical properties of a cereal seed storage protein, C-hordein, and its model peptides

✍ Scribed by Ana M. Gil; Keiko Masui; Akira Naito; A. S. Tatham; P. S. Belton; Hazime Saitô

Publisher: Wiley (John Wiley & Sons)
Year: 1997
Tongue: English
Weight: 818 KB
Volume: 41
Category: Article
ISSN: 0006-3525
DOI: 10.1002/(sici)1097-0282(199703)41:3<289::aid-bip4>3.0.co;2-o

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✦ Synopsis

U'e have recorded the "C CP-MAS and DD-M.4S ntnr spec [ru of dr~' and h~'dra[ed hur[cs tmwge pro!ein, C-hm-dein, us u model,fbr wheat S-poor ptwlatn ins, tqge(her n'ith those oj'rnode[ s?wthet\c pep! ides (Pro): (Gln)6 (I) and (Pro-Gln-Gln-Pro-Phe -Pro-Gln-Glnj 1(II) under dr? or hydrated conditions. The .~pt>(tral,fiatl lre.v @ C-hordein as well as these peptides n'ere apprecia-bl~dlflerent ,jiwm each other depending on the e.rten( of h~ 'dration, retlec[ing dlfltirent domains that adopt d@zwt [.Ispc~@ conjbrmalions as ~'ell as d! 'namics. In particular, considerable proportions oft he peak in[ensi(ies ~ere lost in the CP-MA S spec[ra, and well-resolved l-' C-nmr

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