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Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements
The small all-β protein tendamistat folds and unfolds with two-state kinetics. We determined the volume changes associated with the folding process by performing kinetic and equilibrium measurements at variable pressure between 0.1 and 100 MPa (1 to 1,000 bar). GdmCl-induced equilibrium unfolding tr...
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| Autores principales: | , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
The National Academy of Sciences
2000
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC26608/ https://ncbi.nlm.nih.gov/pubmed/10618363 |
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