Literature DB >> 25640895

Analysis of protein ligand-receptor binding by photoaffinity cross-linking.

Ling Wu1, Bin Xu1.   

Abstract

Photoaffinity cross-linking is a rapidly developing technology for studying biomolecular interactions, including protein ligand-receptor binding. This technology provides detailed binding information including receptor contact sites, active conformation of receptor-ligand complexes, global binding surfaces, and binding modes. Advancements in genetic technology have enabled non-natural photoactive amino acid derivatives to be incorporated into designer or target proteins, providing a host of new opportunities for manufacturing protein photo-probes while bypassing the traditional peptide or small protein limits of classical chemical synthesis. This unit provides several protocols for performing basic photoaffinity cross-linking and related analyses for applications in ligand-receptor binding and protein-protein interactions.
Copyright © 2015 John Wiley & Sons, Inc.

Keywords:  biosynthetic photo-probe; ligand-receptor binding; mapping of binding sites; photoaffinity cross-linking; protein-protein interaction

Mesh:

Substances:

Year:  2015        PMID: 25640895     DOI: 10.1002/0471140864.ps1926s79

Source DB:  PubMed          Journal:  Curr Protoc Protein Sci        ISSN: 1934-3655


  1 in total

1.  Structural insight into host plasma membrane association and assembly of HIV-1 matrix protein.

Authors:  Halilibrahim Ciftci; Hiroshi Tateishi; Kotaro Koiwai; Ryoko Koga; Kensaku Anraku; Kazuaki Monde; Çağdaş Dağ; Ebru Destan; Busra Yuksel; Esra Ayan; Gunseli Yildirim; Merve Yigin; F Betul Ertem; Alaleh Shafiei; Omur Guven; Sabri O Besler; Raymond G Sierra; Chun Hong Yoon; Zhen Su; Mengling Liang; Burcin Acar; Turkan Haliloglu; Masami Otsuka; Fumiaki Yumoto; Mikako Fujita; Toshiya Senda; Hasan DeMirci
Journal:  Sci Rep       Date:  2021-08-04       Impact factor: 4.379

  1 in total

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