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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...

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Detaylı Bibliyografya
Asıl Yazarlar: Krowarsch, Daniel, Otlewski, Jacek
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Cold Spring Harbor Laboratory Press 2001
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2373960/
https://ncbi.nlm.nih.gov/pubmed/11274462
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