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-Reference-Cited by-同舟云学术

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

Published:1991-12 Issue:2-3 Volume:158 Page:353-382
ISSN:0301-0104
Container-title:Chemical Physics
language:en
Short-container-title:Chemical Physics

Author:

Harris Danni L.,Hudson Bruce S.

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference52 articles.

1. Subnanosecond motions of tryptophan residues in proteins

2. 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 study

3. Fluorescence lifetime quenching and anisotropy studies of ribonuclease T1

4. Picosecond time-resolved fluorescence of ribonuclease T1. A pH and substrate analogue binding study

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