Structures and functions of proteins and nucleic acids in protein biosynthesis
作者:
Tatsuo Miyazawa,
Shigeyuki Yokoyama,
期刊:
International Reviews in Physical Chemistry
(Taylor Available online 1989)
卷期:
Volume 8,
issue 2-3
页码: 125-145
ISSN:0144-235X
年代: 1989
DOI:10.1080/01442358909353226
出版商: Taylor & Francis Group
数据来源: Taylor
摘要:
Infrared and Raman spectroscopy is useful for studying helical conformations of polypeptides, which are determined by molecular structure parameters. Nuclear magnetic resonance spectroscopy, as well as X-ray analysis, is now established to be important for conformation studies of proteins and nucleic acids in solution. This article is mainly concerned with the conformational aspect and function regulation in protein biosynthesis. The strict recognition of transfer ribonucleic acid (tRNA) by aminoacyl-tRNA synthetase (ARS) is achieved by multi-step mutual adaptation. The conformations of ARS-bound amino acids have been elucidated by transferred nuclear Overhauser effect analysis. Aminoacyl-tRNA takes the 3′-isomeric form in the polypeptide chain elongation cycle. The regulation of codon recognition by post-transcriptional modification is achieved by conversion of the conformational characteristic of the anticodon of tRNA. The cytidine → lysidine modification of the anticodon of minor isoleucine tRNA concurrently converts the amino acid specificity and the codon specificity. As novel protein engineering, a basic strategy has been established forin vivobiosynthesis of proteins that are substituted with unnatural amino acids (alloproteins).
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