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Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two-dimensional nuclear magnetic resonance.

Structural perturbations due to a series of mutations at the 30-51 disulfide bond of bovine pancreatic trypsin inhibitor have been explored using NMR. The mutants replaced cysteines at positions 30 and 51 by alanine at position 51 and alanine, threonine, or valine at position 30. Chemical shift chan...

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Hlavní autoři: Hurle, M. R., Eads, C. D., Pearlman, D. A., Seibel, G. L., Thomason, J., Kosen, P. A., Kollman, P., Anderson, S., Kuntz, I. D.
Médium: Artigo
Jazyk:Inglês
Vydáno: Cold Spring Harbor Laboratory Press 1992
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142081/
https://ncbi.nlm.nih.gov/pubmed/1284804
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