Chemical cross-links of proteins by using bifunctional reagents |
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| Affiliation: | 1. Beijing National Laboratory for Molecular Sciences, CAS Key Laboratory of Analytical Chemistry for Living Biosystems, National Centre for Mass Spectrometry in Beijing, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, PR China;2. School of Chemical and Environmental Engineering, China University of Mining and Technology, Beijing 100083, PR China;3. Department of Chemistry, University of Science and Technology of China, Hefei, Anhui 230026, PR China;4. University of Chinese Academy of Sciences, Beijing 100049, PR China;1. Kazan National Research Technological University, 68 Karl Marx Street, Kazan 420015, Russia;2. Lehigh University, 6 E. Packer Ave., Bethlehem, PA 18015, USA |
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| Abstract: | - 1.1. The chemical identification of spatial arrangements of the subunits in oligomeric proteins is exclusively achieved by the analysis of the reaction products of the protein and bifunctional reagents.
- 2.2. Since the pioneer work of Hartman and Wold (Biochemistry6, 2439–2448, 1967) the bifunctional reagent such as bis-imido-esters was first introduced into protein chemistry.
- 3.3. We have listed the non-cleavable and cleavable bis-imido-esters, the N-hydroxy-succinimido-csters and the aryl azides which once photolyzed, become the highly reactive nitrene intermediates.
- 4.4. Different reagents classified as homo- and hetero-bifunctional reagents are also listed.
- 5.5. The advantages and limits of each group as well as their chemical properties are advanced and extensively discussed.
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