Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue.

The structural basis for the stability of N termini of helices has been analyzed by thermodynamic and crystallographic studies of three suitably engineered mutants of the barley chymotrypsin inhibitor 2 with Ser, Gly, or Ala at the N-cap position (residue 31). Each mutant has a well-organized shell...

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Detalles Bibliográficos

Publicado en:	Proc Natl Acad Sci U S A
Principais autores:	Harpaz, Y, Elmasry, N, Fersht, A R, Henrick, K
Formato:	Artigo
Idioma:	Inglês
Publicado:	National Academy of Sciences 1994
Assuntos:	Research Article
Acceso en liña:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC42937/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8278384/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.91.1.311
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