NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability (Q27639572)

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English	NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability	scientific article

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scholarly article

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NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability (English)

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protein structure

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2

object named as

Jacek Otlewski

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author name string

Tomasz Cierpicki

1

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language of work or name

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publication date

23 August 2002

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Journal of Molecular Biology

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321

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4

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647-58

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The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase

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Forces contributing to the conformational stability of proteins

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Structural basis of amino acid alpha helix propensity

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Measurement of the β-sheet-forming propensities of amino acids

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Packing is a key selection factor in the evolution of protein hydrophobic cores

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Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability

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Tyrosine hydrogen bonds make a large contribution to protein stability

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On the size of the active site in proteases. I. Papain

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Analysis of serine proteinase-inhibitor interaction by alanine shaving

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Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI).

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Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases

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Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis

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High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence

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Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases

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A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility

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Use of chemical shifts in macromolecular structure determination

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Crevice‐forming mutants of bovine pancreatic trypsin inhibitor: Stability changes and new hydrophobic surface

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Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine.

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Additivity of mutational effects in proteins

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Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI

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Natural protein proteinase inhibitors and their interaction with proteinases

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10.1016/S0022-2836(02)00620-4

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