Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics

David Robinette, Nouri Neamati, Kenneth B. Tomer, Christoph H. Borchers

Результат исследований: Вклад в журналОбзорная статьярецензирование

63 Цитирования (Scopus)


Protein chemistry, such as crosslinking and photoaffinity labeling, in combination with modern mass spectrometric techniques, can provide information regarding protein-protein interactions beyond that normally obtained from protein identification and characterization studies. While protein crosslinking can make tertiary and quaternary protein structure information available, photoaffinity labeling can be used to obtain structural data about ligand-protein interaction sites, such as oligonucleotide-protein, drug-protein and protein-protein interaction. In this article, we describe mass spectrometry-based photoaffinity labeling methodologies currently used and discuss their current limitations. We also discuss their potential as a common approach to structural proteomics for providing 3D information regarding the binding region, which ultimately will be used for molecular modeling and structure-based drug design.

Язык оригиналаАнглийский
Страницы (с-по)399-408
Число страниц10
ЖурналExpert Review of Proteomics
Номер выпуска4
СостояниеОпубликовано - 2006
Опубликовано для внешнего пользованияДа


Подробные сведения о темах исследования «Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics». Вместе они формируют уникальный семантический отпечаток (fingerprint).