Domain elucidation by mass spectrometry

Structure

Volumn 4, Issue 9, 1996, Pages 1013-1016

  Cohen, Steven L ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030587526     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00108-6     Document Type: Article

References (22)

1. Joachimiak, A. & Sigler, P.B. (1991). Crystallization of protein-DNA complexes. Methods Enzymol. 208, 83-99.
2. Hubbard, S.J., Eisenmenger, F. & Thornton, J.M. (1994). Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3, 757-768.
3. Hillenkamp, F., Karas, M., Beavis, R.C. & Chait, B.T. (1991). Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. A 63, 1193-1203.
4. Chat, B.T. & Kent, S.B.H. (1992). Weighing naked proteins: Practical, high-accuracy mass measurement of peptides and proteins. Science 257, 1885-1894.
5. Zaluzec, E.J., Gage, D.A. & Watson, J.T. (1995). Matrix-assisted laser desorption ionization mass spectrometry: Applications in peptide and protein characterization. Protein Expr. Purif. 6, 109-123.
6. Mann, M. & Talbo, G. (1996). Developments in matrix-assisted laser desorption/ionization peptide mass spectrometry. Curr. Opin Biotechnol. 7, 11-19.
7. Mann, M. & Wilm, M. (1995). Electrospray mass spectrometry for protein characterization. Trends Biol. Sci. 20, 219-224.
8. Blatter, E.E., Ross, W., Tang, H., Course, R. L. & Ebright, R.H. (1994). Domain organization of RNA polymerase α subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding. Cell 78, 889-896.
9. Cohen, S.L., Ferré-D'Amaré, A.R., Burley, S.K. & Chat, B.T. (1995). Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry. Protein Sci. 4, 1088-1099.
10. Blackwood, E.M. & Eisenman, R.N. (1991). Max: a helix-loop-helix protein that forms a sequence-specific DNA-binding complex with Myc. Science 12, 1211-1217.
11. Prendergast, G.C., Lawe, D. & Ziff, E.B. (1991). Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation-sensitive DNA binding and Ras cotransformation. Cell 65, 395-407.
12. Littlewood, T. & Evan, G. (1994). Transcription factors 2: Helix-loop-helix. Protein Profile 1, 639-709.
13. Ferré-D'Amaré, A.R., Prendergast, G.C., Ziff, E.B. & Burley, S.K., (1993). Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363, 38-45.
14. Ferré-D'Amaré, A.R., Pognonec, P., Roeder, R.G. & Burley, S.K. (1995). Structure and function of the b/HLH/Z domain of USF. EMBO J. 13, 180-189.
15. Xie, X., et al., & Burley, S.K. (1996). Structural similarity between TAFs and the heterotetrameric core of the histone octamer. Nature 380, 316-322.
16. Burley, S.K. & Roeder, R.G. (1996). Biochemistry and structural biology of transcription factor IID. Ann. Rev. Biochem. 65, 769-799.
17. Chait, B.T. (1994). Mass spectrometry - a useful tool for the protein X-ray crystallographer and NMR spectroscopist. Structure 2, 465-467.
18. Ferré-D'Amaré, A.R. & Burley, S.K. (1996). Dynamic light scattering as a tool for evaluating crystallizability of macromolecules. Methods Enzymol. 276, in press.
19. Cohen, S.L. & Chait, B.T. (1996). Influence of matrix solution conditions on the MALDI-MS analysis of peptides and proteins. Anal. Chem. 68, 31-37.
20. Brockerhoff, S.E., Edmonds, C.G. & Davis, T.N. (1992). Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry. Protein Sci. 1, 504-516.
21. Zappacosta, F., et al., & Pucci, P. (1996). Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: The case of Minibody. Protein Sci. 5, 802-813.
22. Lee, C.-H., Saksela, K., Mirza, U.A., Chait, B.T. & Kuriyan, J. (1996). Crystal structure of the conserved core of HIV-1 Nef complexed with a Src-family SH3 domain. Cell 85, 931-942.