Tryptophan Rotamer Distribution Revealed for the α-Helix in Tear Lipocalin by Site-Directed Tryptophan Fluorescence-Reference-Cited by-同舟云学术

Tryptophan Rotamer Distribution Revealed for the α-Helix in Tear Lipocalin by Site-Directed Tryptophan Fluorescence

Published:2012-11-02 Issue:45 Volume:116 Page:13381-13388
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

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/jp309318r

Reference44 articles.

1. The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition

2. Galline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand Specificities

3. Cation-π Interactions in Lipocalins: Structural and Functional Implications

4. Principles of Fluorescence Spectroscopy

5. Site-Directed Tryptophan Fluorescence Reveals the Solution Structure of Tear Lipocalin: Evidence for Features That Confer Promiscuity in Ligand Binding

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