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The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase
We have used (15)N- and (2)H-NMR spin relaxation experiments to study the response of backbone and side-chain dynamics when a leucine or valine is substituted for a completely buried phenylalanine residue in the SH3 domain from the Fyn tyrosine kinase. Several residues show differences in the time s...
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| Hoofdauteurs: | , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Cold Spring Harbor Laboratory Press
2004
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2280047/ https://ncbi.nlm.nih.gov/pubmed/15044737 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.03502504 |
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