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ID 34798
本文ファイル
著者
Mimura, Shigefumi
Yamato, Takahisa
Kamiyama, Tadashi
Gekko, Kunihiko
キーワード
Isothermal compressibility
Lysozyme
Molecular evolution
Nonneutral pathway
Normal-mode analysis
Volume fluctuation
NDC
生物科学・一般生物学
抄録(英)
The evolution of structural fluctuations of proteins was examined by calculating the isothermal compressibility (beta(T)) values of chicken lysozyme and its six evolutionary mutants at Thr40, Ile55, and Ser91 (a ternary mutant corresponding to bobwhite lysozyme) from their X-ray structures by normal-mode analysis at 300 K. The Or values of the two extant lysozymes from chicken and bobwhite were 1.61 and 1.59 Mbar(-1), respectively, but five other evolutionary mutants showed larger beta(T) values of up to 2.17 Mbar(-1). These results suggest that ancestral lysozymes exhibit larger volume fluctuations than extant ones, and hence that the molecular evolution of lysozymes has followed a nonneutral evolutionary pathway. The evolutionary mutants contained large amount of cavities, although no change was visible in the X-ray structures. There was a linear correlation between beta(T) and total cavity volume, predicting that the cavity volume or atomic packing is an important factor regulating volume fluctuations during the molecular evolution of this protein. (C) 2011 Elsevier B.V. All rights reserved.
掲載誌名
Biophysical Chemistry
161巻
開始ページ
39
終了ページ
45
出版年月日
2012
出版者
Elsevier Science BV
ISSN
0301-4622
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
(c) 2012 Elsevier B.V. All rights reserved.
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部局名
その他