Senapathy Rajagopalan, Ph.D. - Publications
Affiliations: | 2006 | University of Wisconsin, Madison, Madison, WI |
Area:
Protein folding in the cell and Biomolecular spectroscopyYear | Citation | Score | |||
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2012 | Rajagopalan S, Cavagnero S, Kurt N, Kwon J. Backbone 1H, 13CA, and 15N Chemical Shifts Assignments and 15N T1 and T2 Relaxation Parameters for the N-terminal (1-119) Fragment of sperm whale apomyoglobin in the presence of DnaK-beta Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16218 | 0.631 | |||
2012 | Rajagopalan S, Cavagnero S, Kurt N, Kwon J. Backbone 1H, 13CA, and 15N Chemical Shifts Assignments and 15N T1 and T2 Relaxation Parameters for the N-terminal (1-119) Fragment of sperm whale apomyoglobin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16217 | 0.629 | |||
2011 | Rajagopalan S, Kurt N, Cavagnero S. High-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119. Biophysical Journal. 100: 747-55. PMID 21281590 DOI: 10.1016/J.Bpj.2010.12.3722 | 0.646 | |||
2010 | Fedyukina DV, Rajagopalan S, Sekhar A, Fulmer EC, Eun YJ, Cavagnero S. Contribution of long-range interactions to the secondary structure of an unfolded globin. Biophysical Journal. 99: L37-9. PMID 20816043 DOI: 10.1016/J.Bpj.2010.06.038 | 0.498 | |||
2006 | Chen Z, Kurt N, Rajagopalan S, Cavagnero S. Secondary structure mapping of DnaK-bound protein fragments: chain helicity and local helix unwinding at the binding site. Biochemistry. 45: 12325-33. PMID 17014085 DOI: 10.1021/Bi0612263 | 0.643 | |||
2006 | Kurt N, Rajagopalan S, Cavagnero S. Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain. Journal of Molecular Biology. 355: 809-20. PMID 16309705 DOI: 10.1016/J.Jmb.2005.10.029 | 0.669 | |||
2004 | Rajagopalan S, Chow C, Raghunathan V, Fry CG, Cavagnero S. NMR spectroscopic filtration of polypeptides and proteins in complex mixtures. Journal of Biomolecular Nmr. 29: 505-16. PMID 15243181 DOI: 10.1023/B:Jnmr.0000034354.30702.De | 0.609 | |||
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