A high-resolution 1H-NMR study of human transforming growth factor alpha. Structure and pH-dependent conformational interconversion.
作者： Michael J. TAPPIN , Robert M. COOKE , John E. FITTON , Iain D. CAMPBELL
DOI: 10.1111/J.1432-1033.1989.TB14594.X
关键词:
摘要: The 500-MHz and 600-MHz 1H-NMR spectra of recombinant human transforming growth factor α have been recorded at pH values 3.8, 6.5 9.4. Analysis various two-dimensional has enabled sequence-specific assignments to be made the secondary structure identified. Information on tertiary fold also obtained from observed nuclear Overhauser effects titration histidine residues. overall protein is very similar that epidermal factor, as might expected sequence similarity. However, 3.8 found show interesting differences those two higher pHs factor.
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