生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
43 巻 , 2 号
通巻246号
選択された号の論文の10件中1~10を表示しています
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  • 金谷 茂則
    原稿種別: 研究論文
    専門分野: 情報学
    2003 年 43 巻 2 号 p. 75-80
    発行日: 2003年
    公開日: 2003/03/25
    ジャーナル フリー
    Ribonuclease H specifically cleaves the RNA strand of RNA/DNA hybrids. Based on the difference in the amino acid sequences, RNases H are classified into two major families, Type 1 and Type 2 RNases H. Type 1 and Type 2 RNases H share a common three-dimensional structure despite their poor amino acid sequence similarity. Whether their in vivo functions are cooperative or independent is of great interest. In addition, the enzymes, especially E. coli RNase HI, have been shown to be an excellent model not only for analyzing protein stability and protein folding, but also for protein engineering. I would like to summarize a recent progress in the RNase H studies.
  • 元池 N. 育子
    原稿種別: 研究論文
    専門分野: 情報学
    2003 年 43 巻 2 号 p. 81-86
    発行日: 2003年
    公開日: 2003/03/25
    ジャーナル フリー
    In living organisms, signals propagate through various kinds of geometrical or boundary paths. It is well established that a traveling wave can be generated on an excitable field; this generation is described by reaction-diffusion equations for an activator and inhibitor. I use a numerical simulation to show that the signaling pulse can be transmitted from an excitable field to an opposing excitable field via an intervening passive diffusion field in a characteristic manner that depends upon the spatial geometry of the excitable fields. Using such characteristics, it is possible to design various kinds of simple information operations.
  • M・マイケル・ グロミハ
    原稿種別: 研究論文
    専門分野: 情報学
    2003 年 43 巻 2 号 p. 87-92
    発行日: 2003年
    公開日: 2003/03/25
    ジャーナル フリー
    During the process of protein folding, the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form the stable native structure. The knowledge about interactions between amino acid residues in protein structures is very helpful to understand the mechanism of protein folding and stability. In this review, I classify the inter-residue interactions into short, medium and long range based on a simple geometric approach. The features of these interactions in different structural classes and folding types of globular proteins have been delineated. Further, the development of a new parameter, long-range order, based on inter-residue interactions and its application for predicting the protein folding rates are highlighted. The information gained from the studies on inter-residue interactions provides valuable insights for understanding protein folding and de novo protein design.
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