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...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
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| Päätekijät: | , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
1994
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| Aiheet: | |
| Linkit: | 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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