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Destabilizing Mutations Alter the Hydrogen Exchange Mechanism in Ribonuclease A
The effect of strongly destabilizing mutations, I106A and V108G of Ribonuclease A (RNase A), on its structure and stability has been determined by NMR. The solution structures of these variants are essentially equivalent to RNase A. The exchange rates of the most protected amide protons in RNase A (...
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| Glavni autori: | , , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
The Biophysical Society
2008
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| Teme: | |
| Online pristup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2257908/ https://ncbi.nlm.nih.gov/pubmed/18192347 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.107.122952 |
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