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Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in the solid state.

Streptomyces subtilisin inhibitor (SSI) contains three methionine residues in a subunit: two (at positions 73 and 70) in the crucial enzyme-recognition sites P1 and P4, respectively, and one (Met 103) in the hydrophobic core. The motions of the side chains of these three Met residues and the changes...

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Autors principals: Tamura, A., Matsushita, M., Naito, A., Kojima, S., Miura, K. I., Akasaka, K.
Format: Artigo
Idioma:Inglês
Publicat: Cold Spring Harbor Laboratory Press 1996
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143239/
https://ncbi.nlm.nih.gov/pubmed/8771205
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