doi: 10.1016/0003-2697(91)90127-f.
A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system
Affiliations
- PMID: 1888025
- DOI: 10.1016/0003-2697(91)90127-f
Item in Clipboard
A mass spectrometry method for mapping the interface topography of interacting proteins, illustrated by the melittin-calmodulin system
Anal Biochem.
1991 Jul.
Abstract
The shielding of lysine groups from acetylation by acetic anhydride has been used to identify the regions of calmodulin in contact with melittin in the 1:1 complex. The estimation of the degree of acetylation was done by examining cyanogen bromide and cyanogen bromide/trypsin digests by mass spectrometry. Evidence was obtained that lysines-21, -75, and -148 are protected to some extent, with the implication that both the N- and C-terminal lobes and the connecting strand are involved in the interaction.
Similar articles
-
Mapping the topology and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTICRMS: direct demonstration of multiple binding modes.Biochemistry. 2004 Apr 27;43(16):4703-15. doi: 10.1021/bi036149f. Biochemistry. 2004. PMID: 15096039
-
Topology of the calmodulin-melittin complex.J Mol Biol. 1998 Apr 10;277(4):945-58. doi: 10.1006/jmbi.1998.1629. J Mol Biol. 1998. PMID: 9545383
-
Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry.J Am Soc Mass Spectrom. 2005 Feb;16(2):225-33. doi: 10.1016/j.jasms.2004.11.009. J Am Soc Mass Spectrom. 2005. PMID: 15694772
-
Mass spectrometry of peptides, proteins and glycoproteins.J Chem Technol Biotechnol. 1991;51(1):127-33. doi: 10.1002/jctb.280510116. J Chem Technol Biotechnol. 1991. PMID: 1367517 Review. No abstract available.
-
Mapping phosphorylation sites in proteins by mass spectrometry.Methods Enzymol. 2002;351:279-96. doi: 10.1016/s0076-6879(02)51853-x. Methods Enzymol. 2002. PMID: 12073350 Review. No abstract available.
Cited by
-
Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chem Rev. 2020 May 27;120(10):4355-4454. doi: 10.1021/acs.chemrev.9b00815. Epub 2020 Apr 22. Chem Rev. 2020. PMID: 32319757 Free PMC article. Review.
-
Surface topology of Minibody by selective chemical modifications and mass spectrometry.Protein Sci. 1997 Sep;6(9):1901-9. doi: 10.1002/pro.5560060911. Protein Sci. 1997. PMID: 9300490 Free PMC article.
-
Characterization of a discontinuous epitope of the HIV envelope protein gp120 recognized by a human monoclonal antibody using chemical modification and mass spectrometric analysis.J Am Soc Mass Spectrom. 2010 Oct;21(10):1687-98. doi: 10.1016/j.jasms.2010.03.031. Epub 2010 Mar 31. J Am Soc Mass Spectrom. 2010. PMID: 20434359 Free PMC article.
-
Structural characterization of the conformational change in calbindin-D28k upon calcium binding using differential surface modification analyzed by mass spectrometry.Biochemistry. 2009 Sep 15;48(36):8603-14. doi: 10.1021/bi900350q. Biochemistry. 2009. PMID: 19658395 Free PMC article.
-
Quantitative profiling of histone post-translational modifications by stable isotope labeling.Methods. 2007 Mar;41(3):312-9. doi: 10.1016/j.ymeth.2006.08.017. Methods. 2007. PMID: 17309842 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
