How Do Rotameric Conformations Influence the Time-Resolved Fluorescence of Tryptophan in Proteins? A Perspective Based on Molecular Modeling and Quantum Chemistry-Reference-Cited by-同舟云学术

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How Do Rotameric Conformations Influence the Time-Resolved Fluorescence of Tryptophan in Proteins? A Perspective Based on Molecular Modeling and Quantum Chemistry

Published:2008-10-01 Issue:5 Volume:9 Page:427-446
ISSN:1389-2037
Container-title:Current Protein & Peptide Science
language:en
Short-container-title:CPPS

Author:

Moors Samuel,Jonckheer Abel,De Maeyer Marc,Engelborghs Yves,Ceulemans Arnout

Publisher

Bentham Science Publishers Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,General Medicine

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Orientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptide;Royal Society Open Science;2016-10

2. In vitro evaluation of the conjugations of neonicotinoids with transport protein: photochemistry, ligand docking and molecular dynamics studies;RSC Advances;2016

3. Reorientations of Aromatic Amino Acids and Their Side Chain Models: Anisotropy Measurements and Molecular Dynamics Simulations;The Journal of Physical Chemistry A;2009-10-29

4. Tryptophan Conformations Associated with Partial Unfolding in Ribonuclease T1;Biophysical Journal;2009-09

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