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References

This article has been cited by other articles in PMC.

Abstract A procedure for the dynamical simulation of activated processes, such as ligand binding and enzymatic reactions, in a globular protein is outlined. Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C. FEBS Lett. Complete tyrosine assignments in the high field 1H nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitor.

Activated barrier crossing : applications in physics, chemistry and biology - Semantic Scholar

Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor BPTI. Biophys Struct Mech. Dynamics of ligand binding to myoglobin. Dynamics of folded proteins. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng. Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor.

Semi-empirical energy calculations. Protein structural fluctuations during a period of ps. Picosecond dynamics of tyrosine side chains in proteins.

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Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment. How does Europe PMC derive its citations network? Protein Interactions. Protein Families. Hochstrasser, Chem.


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Waldeck and G. Russo and P. Thistlewaite, Chem. Tredwell and A. Osborne, J. Faraday Trans. Robinson, W. Jalenak, and D. Statman, Chem. Statman and G.