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Amino-acid substitutions at the fully exposed P(1) site of bovine pancreatic trypsin inhibitor affect its stability
It is widely accepted that solvent-exposed sites in proteins play only a neglible role in determining protein energetics. In this paper we show that amino acid substitutions at the fully exposed Lys15 in bovine pancreatic trypsin inhibitor (BPTI) influenced the CD- and DSC-monitored stability: The T...
Tallennettuna:
| Päätekijät: | , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2001
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2373960/ https://ncbi.nlm.nih.gov/pubmed/11274462 |
| Tagit: |
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