Fluorescence and molecular dynamics study of the internal motion of the buried tryptophan in bacteriophage T4 lysozyme: Effects of temperature and alteration of nonbonded networks
- 1 December 1991
- journal article
- Published by Elsevier in Chemical Physics
- Vol. 158 (2-3) , 353-382
- https://doi.org/10.1016/0301-0104(91)87077-9
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- Picosecond tryptophan fluorescence of thioredoxin: evidence for discrete species in slow exchangeBiochemistry, 1989
- Nanosecond dynamics of horse heart apocytochrome c in aqueous solution as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59)Biochemistry, 1988
- Rotational dynamics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex. A steady-state and time-resolved anisotropy studyBiochemistry, 1988
- Molecular dynamics simulations of ribonuclease T1: analysis of the effect of solvent on the structure, fluctuations, and active site of the free enzymeBiochemistry, 1988
- Picosecond time-resolved fluorescence of ribonuclease T1. A pH and substrate analogue binding studyBiophysical Journal, 1987
- Internal motion and electron transfer in proteins: a picosecond fluorescence study of three homologous azurinsBiochemistry, 1987
- Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolutionJournal of Molecular Biology, 1987
- Fluorescence lifetime quenching and anisotropy studies of ribonuclease T1Biochemistry, 1985
- Side-chain rotational isomerization in proteins: a mechanism involving gating and transient packing defectsJournal of the American Chemical Society, 1983
- Subnanosecond motions of tryptophan residues in proteinsProceedings of the National Academy of Sciences, 1979