清华大学 生物核磁共振波谱学(英文)wuthrich-the second decade.doc

清华大学 生物核磁共振波谱学(英文)wuthrich-the second decade.doc

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清华大学 生物核磁共振波谱学(英文)wuthrich-the second decade

清华大学:生物核磁共振波谱学(英文):wuthrich-the second decade 分类:生物 格式:pdf 日期:2006年02月22日 备注:本文章/文件仅为课件“清华大学:生物核磁共振波谱学(英文)”(或其中一个章节)的简单文本/文件预览版,可能不包括课件的图片、视频、音频、动画等相关素材,本文章/文件与课件详细内容可能有较大差异,部分音视频、flash等多媒体文件可能因客户端没有安装相关插件而无法预览,建议用户下载完整版课件。 NMR supplement 492 nature structural biology ? NMR supplement ? july 1998 used for quantitative characterization of structural and dynamic aspects of protein and nucleic acid hydration in solution. NMR data on dynamics and solvation have so far in most instances been collect- ed with small proteins and nucleic acid fragments, but this fundamental informa- tion applies to any molecular size and can be used for the interpretation of crystal structures with regard to structure-func- tion correlations in physiological fluids 9 . However, although NMR data on molecu- lar dynamics have long attracted keen interest by theoreticians 10,11 , the inherent complexities of dynamic macromolecular struc- tures have so far limited the use of this information in the prac- tice of analyzing biochemical measurements and designing novel projects. In a certain sense these NMR data — on dynamics and solvation — appear to be ahead of their time: here, then, is an open avenue for the future. Very recent observations also indi- cate that our view of internal mobility of proteins may still be largely incomplete and that additional insight on low frequency motions can be anticipated from novel NMR approaches 12–14 , in particular also from the residual anisotropic interac- tions reviewed by Prestegard 15 in his contribution to this volume. NMR spectroscopy is special among the techniques of structural biology in its abil- ity to observe and characterize unfolded polypeptide chains in solution 16,17 . Applications of interest to the ‘protein folding problem’ are discussed in the pre- sent NMR special issue in articles by Dyson and Wright 18 , and by Dobson and Hore 19 . In addition, recent structure determinations revealed the existence of In the first Nature Structural Bi

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