Crevice-forming mutants of bovine pancreatic trypsin inhibitor: stability changes and new hydrophobic surface
about
Interatomic potentials and solvation parameters from protein engineering data for buried residuesThermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation.Thermodynamics of BPTI foldingMutational analysis of the BPTI folding pathway: I. Effects of aromatic-->leucine substitutions on the distribution of folding intermediatesThermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI).Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability.Heat capacity changes upon burial of polar and nonpolar groups in proteins.Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A.
P2860
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P2860
Crevice-forming mutants of bovine pancreatic trypsin inhibitor: stability changes and new hydrophobic surface
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
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1993年学术文章
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1993年学术文章
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1993年学术文章
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name
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@ast
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@en
type
label
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@ast
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@en
prefLabel
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@ast
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@en
P2093
P2860
P356
P1433
P1476
Crevice-forming mutants of bov ...... es and new hydrophobic surface
@en
P2093
A T Danishefsky
A Wlodawer
C Woodward
P2860
P304
P356
10.1002/PRO.5560020410
P577
1993-04-01T00:00:00Z