Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor.

In the absence of specific interactions, the relative attenuation of protein NMR signals due to added stable free radicals such as TEMPOL should reflect the solvent accessibility of the molecular surface. The quantitative correlation between observed attenuation and surface accessibility was investi...

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Main Authors: Molinari, H, Esposito, G, Ragona, L, Pegna, M, Niccolai, N, Brunne, R M, Lesk, A M, Zetta, L
格式: Artigo
語言:Inglês
出版: 1997
主題:
Research Article
在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC1180939/
https://ncbi.nlm.nih.gov/pubmed/9199802
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