The Folding of Spectrin Domains II: Phi-value Analysis of R16
| Autor: | Jane Clarke, Kathryn A. Scott, Lucy G. Randles |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Denaturation Protein Folding Phi value analysis Protein Engineering Curvature Protein Structure Secondary Drug Stability Structural Biology Animals Spectrin Molecular Biology Brain Chemistry Chemistry Protein engineering Recombinant Proteins Chevron plot Protein Structure Tertiary Folding (chemistry) Kinetics Crystallography Mutagenesis Site-Directed Biophysics Thermodynamics Protein folding Chickens |
| Zdroj: | Journal of Molecular Biology. 344:207-221 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2004.09.023 |
| Popis: | Studies on the folding of helical proteins have shown a wide range of different mechanisms and highlighted the importance of helical propensity as a factor in determining folding mechanism. Here, we contribute to this interesting field with the protein engineering phi-value analysis of the 16th domain of chicken brain alpha-spectrin, R16. The fortuitous curvature seen in the unfolding arm of the chevron plot allows us to investigate both early and late events in folding. R16 is the first two-state helical protein for which this has been possible. |
| Databáze: | OpenAIRE |
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