Laser-Raman and FT-IR spectroscopic studies of peptide-analogues of silkmoth chorion protein segments

被引：23

作者：

Benaki, DC

Aggeli, A

Chryssikos, GD

Yiannopoulos, YD

Kamitsos, EI

Brumley, E

Case, ST

Boden, N

Hamodrakas, SJ ^{[1
]}

机构：

[1] Univ Athens, Dept Biol, Div Cell Biol & Biophys, GR-15701 Athens, Greece

[2] Univ Leeds, Sch Chem, Ctr Self Organizing Mol Syst, Leeds LS2 9JT, W Yorkshire, England

[3] Natl Hellen Res Fdn, Inst Theoret & Phys Chem, GR-11635 Athens, Greece

[4] Univ Mississippi, Med Ctr, Dept Biochem, Jackson, MS 39216 USA

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 1998年 / 23卷 / 01期

关键词：

structure; peptide-analogues; silkmoth chorion proteins; Laser-Raman spectroscopy; FT-IR spectroscopy;

D O I：

10.1016/S0141-8130(98)00032-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Silkmoth chorion, the proteinaceous major component of the eggshell, with extraordinary mechanical and physiological properties, consists of a complex set of proteins, which have a tripartite structure: a central, evolutionarily conserved, domain and two more variable 'arms'. Peptide-analogues of silkmoth chorion protein central domain segments have been synthesized. Laser-Raman and infrared spectroscopic studies suggest the preponderance of antiparallel beta-pleated sheet structure for these peptides, both in solution and in the solid state. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：49 / 59

页数：11

共 24 条

[1] THE SOLUTION STRUCTURE OF CONCANAVALIN-A PROBED BY FT-IR SPECTROSCOPY [J].