Identification of peptide-binding sites within BSA using rapid, laser-induced covalent cross-linking combined with high-performance mass spectrometry-Reference-Cited by-同舟云学术

Identification of peptide-binding sites within BSA using rapid, laser-induced covalent cross-linking combined with high-performance mass spectrometry

Published:2017-10-10 Issue:2 Volume:31 Page:e2680
ISSN:0952-3499
Container-title:Journal of Molecular Recognition
language:en
Short-container-title:J Mol Recognit

Author:

Hauser Melinda¹,Qian Chen²³,King Steven T.²⁴,Kauffman Sarah¹,Naider Fred⁵⁶,Hettich Robert L.²³^ORCID,Becker Jeffrey M.¹^ORCID

Affiliation:

1. Department of Microbiology; University of Tennessee; Knoxville TN USA

2. Chemical Science Division; Oak Ridge National Laboratory; Oak Ridge TN USA

3. UT-ORNL Graduate School of Genome Science and Technology; University of Tennessee; Knoxville TN USA

4. Department of Chemistry; University of Tennessee; Knoxville TN USA

5. Department of Chemistry and Macromolecular Assemblies Institute; College of Staten Island, CUNY; New York NY USA

6. Programs in Biochemistry and Chemistry, Graduate Center; The City University of New York; New York NY USA

Funder

National Institute of General Medical Sciences

Publisher

Wiley

Subject

Molecular Biology,Structural Biology

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3. p-Benzoyl-L-phenylalanine, a new photoreactive amino acid. Photolabeling of calmodulin with a synthetic calmodulin-binding peptide;Kauer;J Biol Chem,1986

4. Photoaffinity labeling of peptide hormone receptors;Hazum;Endocr Rev,1983

5. Photoaffinity labeling of biological systems;Chowdhry;Annu Rev Biochem,1979

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