Modulation of p-Cyanophenylalanine Fluorescence by Amino Acid Side Chains and Rational Design of Fluorescence Probes of α-Helix Formation-Reference-Cited by-同舟云学术

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Modulation of p-Cyanophenylalanine Fluorescence by Amino Acid Side Chains and Rational Design of Fluorescence Probes of α-Helix Formation

Published:2010-07-02 Issue:29 Volume:49 Page:6290-6295
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Taskent-Sezgin Humeyra¹,Marek Peter¹,Thomas Rosanne¹,Goldberg Daniel¹,Chung Juah¹,Carrico Isaac¹²³,Raleigh Daniel P.¹²³

Affiliation:

1. Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

2. Institute of Chemical Biology and Drug Discovery, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

3. Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, Stony Brook, New York 11794

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi100932p

Reference26 articles.

1. Principles of Fluorescence Spectroscopy

2. TIME-RESOLVED FLUORESCENCE OF PROTEINS

3. [8] Enhancement of protein spectra with tryptophan analogs: Fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions

4. Incorporation of Tryptophan Analogues into Staphylococcal Nuclease, Its V66W Mutant, and Δ137−149 Fragment: Spectroscopic Studies

5. [4] Fluorescent amino acid analogs

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