Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.
about
Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.Analysis of serine proteinase-inhibitor interaction by alanine shaving.Molecular characterization of Ancylostoma ceylanicum Kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay.Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex.Quinary interactions with an unfolded state ensemble.Fluorine teams up with water to restore inhibitor activity to mutant BPTI.
P2860
Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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name
Amino-acid substitutions at th ...... nhibitor affect its stability.
@en
type
label
Amino-acid substitutions at th ...... nhibitor affect its stability.
@en
prefLabel
Amino-acid substitutions at th ...... nhibitor affect its stability.
@en
P2860
P356
P1433
P1476
Amino-acid substitutions at th ...... nhibitor affect its stability.
@en
P2093
D Krowarsch
J Otlewski
P2860
P304
P356
10.1110/PS.38101
P577
2001-04-01T00:00:00Z