Probing the Folding Preferences in HIV-1 Protease and Its Precursor

来源 :2005 World DNA and Genome Day(2005中国(大连)国际DNA和基因组节大会) | 被引量 : 0次 | 上传用户:btly540205390
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  In the present post genomic era where structural genomics has occupied the center stage of NMR research,there is a high demand on the speed of resonance assignment and structure determination,whereas,the presently available methods based either on NOESY or on some triple resonance experiments are rather slow.They also have limited success with unfolded proteins because of lack of NOEs,and poor dispersion of amide and carbon chemical shifts.Here we describe an efficient approach to rapid resonance assignment suitable for both folded and unfolded proteins,making use of the triple resonance experiments HNN and HN(C)N recently described.
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