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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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Bibliografische gegevens
Hoofdauteurs: Scott, Kathryn A., Alonso, Darwin O. V., Sato, Satoshi, Fersht, Alan R., Daggett, Valerie
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: National Academy of Sciences 2007
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Online toegang: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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