Double Tryptophan Exciton Probe to Gauge Proximal Side Chains in Proteins: Augmentation at Low Temperature-Reference-Cited by-同舟云学术

Double Tryptophan Exciton Probe to Gauge Proximal Side Chains in Proteins: Augmentation at Low Temperature

Published:2015-03-02 Issue:10 Volume:119 Page:3962-3968
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Gasymov Oktay K.¹,Abduragimov Adil R.¹,Glasgow Ben J.¹

Affiliation:

1. Departments of Pathology and Ophthalmology and Jules Stein Eye Institute, University California at Los Angeles, Los Angeles, California 90095, United States

Funder

National Eye Institute

Jules Stein Eye Institute, University of California, Los Angeles

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp512864s

Reference35 articles.

1. Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR

2. Distance Measurements in the Nanometer Range by Pulse EPR

3. Toward the Fourth Dimension of Membrane Protein Structure: Insight into Dynamics from Spin-Labeling EPR Spectroscopy

4. Fluorescence Resonance Energy Transfer Spectroscopy Is a Reliable "Ruler" for Measuring Structural Changes in Proteins

5. Site-directed circular dichroism of proteins: 1Lb bands of Trp resolve position-specific features in tear lipocalin

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