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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Bibliografische gegevens
Hoofdauteurs: Molinari, H, Esposito, G, Ragona, L, Pegna, M, Niccolai, N, Brunne, R M, Lesk, A M, Zetta, L
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1997
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Research Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1180939/
https://ncbi.nlm.nih.gov/pubmed/9199802
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