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Conformational entropy of alanine versus glycine in protein denatured states
The presence of a solvent-exposed alanine residue stabilizes a helix by 0.4–2 kcal·mol(−1) relative to glycine. Various factors have been suggested to account for the differences in helical propensity, from the higher conformational freedom of glycine sequences in the unfolded state to hydrophobic a...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1815238/ https://ncbi.nlm.nih.gov/pubmed/17307875 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0611182104 |
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