Fluorescent Ribonucleoside as a FRET Acceptor for Tryptophan in Native Proteins-Reference-Cited by-同舟云学术

Fluorescent Ribonucleoside as a FRET Acceptor for Tryptophan in Native Proteins

Published:2010-08-09 Issue:34 Volume:132 Page:11896-11897
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Xie Yun¹,Maxson Tucker¹,Tor Yitzhak¹

Affiliation:

1. Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja105244t

Reference28 articles.

1. Evolution of Amino Acid Frequencies in Proteins Over Deep Time: Inferred Order of Introduction of Amino Acids into the Genetic Code

2. Role of aromatic amino acids in protein-nucleic acid recognition

3. Trp (1.02% average amino acid composition; ref1) is 1.74 times more frequently found at RNA binding sites than protein surfaces, while Phe’s value is the same. Trp is also 2.56 times more frequently found at RNA binding sites than DNA binding sites (ref2).

4. Fluorescent Analogs of Biomolecular Building Blocks: Design, Properties, and Applications

5. Lakowicz, J. R.Principles of fluorescence spectroscopy,3rd. ed.;Springer:New York, 2006; pp530−535.

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