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Material Transfer Agreement form to be filed with requests for plasmids etc The lab's research interests focus on the structural biology complex dynamic systems. Major foci -- 1) protein domains in intracellular signal transduction, including SH2, SH3, kinase, phosphatase, PH domains, and many others and how natural ligands interact with them. Signaling disorders related to these domains lead to many disease states. 2) Dynamic processes associated with nuclear transport. 3) An additional area of interest is the development of NMR and related methods for structural biology. Developmental projects include segmental labeling, other novel isotopic labeling methods, novel use of molecular dynamics simulation, small angle scattering by X-rays and neutrons, and detection of protein-protein interaction surfaces and dynamics.
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There is an immediate opening for a postdoctoral researcher

in my lab at Albert Einstein College of Medicine, Department of Biochemistry. This is for our projects, see references below, on (1) the molecular mechanism of rapid and selective transport in the nuclear pore complex, funded by NIH, and using NMR, biophysical chemistry, protein engineering, and simulations (recent publications below); (2) split inteins that mediate the protein ligation process with unprecedented speed and fidelity, creating enormous potential in protein biotechnology with applications ranging from basic molecular and cell biology to the preparation of protein therapeutics. You will have access to the outstanding facilities of the NYSBC, and the Einstein Structural NMR Core.
Interested candidates with expertise (PhD, or about to complete) in biomolecular NMR and experience in protein biochemistry and biophysics should email me a biographical sketch including the names of three references.
1. Dixit U, Bhutoria S, Wu X, Qiu L, Spira M, Mathew S, Harris R, Adams LJ, Cahill S, Pathak R, Rajesh Kumar P, Nguyen M, Acharya SA, Brenowitz M, Almo SC, Zou X, Steven AC, Cowburn D, Girvin M, Kalpana GV. INI1/SMARCB1 Rpt1 domain mimics TAR RNA in binding to integrase to facilitate HIV-1 replication. Nat Commun. 2021;12(1):2743. Epub 2021/05/14. doi: 10.1038/s41467-021-22733-9. PubMed PMID: 33980829; PMCID: PMC8115288.
2. Sparks S, Hayama R, Rout MP, Cowburn D. Analysis of Multivalent IDP Interactions: Stoichiometry, Affinity, and Local Concentration Effect Measurements. Methods in molecular biology (Clifton, NJ. 2020;2141:463-75. Epub 2020/07/23. doi: 10.1007/978-1-0716-0524-0_23. PubMed PMID: 32696372.
3. Bravo-Ferreira JF, Cowburn D, Khoo Y, Singer A. NMR Assignment through Linear Programming. arXiv preprint arXiv:200803641. 2020.
4. Cable J, Brangwynne C, Seydoux G, Cowburn D, Pappu RV, Castaneda CA, Berchowitz LE, Chen Z, Jonikas M, Dernburg A, Mittag T, Fawzi NL. Phase separation in biology and disease-a symposium report. Ann N Y Acad Sci. 2019;1452(1):3-11. Epub 2019/06/15. doi: 10.1111/nyas.14126. PubMed PMID: 31199001; PMCID: PMC6751006.
5. Stevens AJ, Sekar G, Gramespacher JA, Cowburn D, Muir TW. An Atypical Mechanism of Split Intein Molecular Recognition and Folding. J Am Chem Soc. 2018;140(37):11791-9. Epub 2018/08/30. doi: 10.1021/jacs.8b07334. PubMed PMID: 30156841; PMCID: PMC7232844.
6. Sparks S, Temel DB, Rout MP, Cowburn D. Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering. Structure. 2018;26(3):477-84 e4. Epub 2018/02/13. doi: 10.1016/j.str.2018.01.010. PubMed PMID: 29429880; PMCID: PMC5929991.
7. Hayama R, Sparks S, Hecht LM, Dutta K, Karp JM, Cabana CM, Rout MP, Cowburn D. Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex. J Biol Chem. 2018;293(12):4555-63. Epub 2018/01/28. doi: 10.1074/jbc.AC117.001649. PubMed PMID: 29374059; PMCID: PMC5868264.
8. Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D. Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nat Commun. 2017;8(1):2215. Epub 2017/12/22. doi: 10.1038/s41467-017-02308-3. PubMed PMID: 29263320; PMCID: PMC5738438.
9. Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J. Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure. 2017;25(3):434-45. Epub 2017/02/07. doi: 10.1016/j.str.2017.01.006. PubMed PMID: 28162953; PMCID: PMC5342941.
10. Stevens AJ, Sekar G, Shah NH, Mostafavi AZ, Cowburn D, Muir TW. A promiscuous split intein with expanded protein engineering applications. Proc Natl Acad Sci U S A. 2017;114(32):8538-43. Epub 2017/07/26. doi: 10.1073/pnas.1701083114. PubMed PMID: 28739907; PMCID: PMC5559002.
11. Karp JM, Sparks S, Cowburn D. Effects of FGFR2 kinase activation loop dynamics on catalytic activity. PLoS computational biology. 2017;13(2):e1005360. Epub 2017/02/06. doi: 10.1371/journal.pcbi.1005360. PubMed PMID: 28151998; PMCID: PMC5313233.
12. Stevens AJ, Brown ZZ, Shah NH, Sekar G, Cowburn D, Muir TW. Design of a Split Intein with Exceptional Protein Splicing Activity. J Am Chem Soc. 2016;138(7):2162-5. Epub 2016/02/09. doi: 10.1021/jacs.5b13528. PubMed PMID: 26854538; PMCID: PMC4894280.
13. Raveh B, Karp JM, Sparks S, Dutta K, Rout MP, Sali A, Cowburn D. Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex. Proc Natl Acad Sci U S A. 2016;113(18):E2489-97. Epub 2016/04/20. doi: 10.1073/pnas.1522663113. PubMed PMID: 27091992; PMCID: PMC4983827.

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David Cowburn, Ph.D., D.Sc., Professor, Depts of Biochemistry, and of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, US. T +19089130495 cowburn@cowburnlab.org.