Peter L. Privalov
Affiliations: | 1991- | Johns Hopkins University, Baltimore, MD |
Area:
General Biophysics, Biochemistry, Molecular BiologyWebsite:
http://bio.jhu.edu/directory/peter-privalov/Google:
"Peter Privalov"Bio:
https://prabook.com/web/peter_l.privalov/70405
https://www.researchgate.net/profile/Peter_Privalov
Mean distance: (not calculated yet)
Children
Sign in to add trainee| Zhenlan Li | grad student | 2003 | Johns Hopkins |
| George I. Makhatadze | post-doc | 1992 | Johns Hopkins (Chemistry Tree) |
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Publications
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| Privalov PL, Crane-Robinson C. (2020) Forces maintaining the DNA double helix. European Biophysics Journal : Ebj |
| Dragan A, Privalov P, Crane-Robinson C. (2019) Thermodynamics of DNA: heat capacity changes on duplex unfolding. European Biophysics Journal : Ebj. 48: 773-779 |
| Privalov PL, Crane-Robinson C. (2018) Forces maintaining the DNA double helix and its complexes with transcription factors. Progress in Biophysics and Molecular Biology |
| Privalov PL, Crane-Robinson C. (2018) Translational Entropy and DNA Duplex Stability. Biophysical Journal. 114: 15-20 |
| Privalov PL, Crane-Robinson C. (2016) Role of water in the formation of macromolecular structures. European Biophysics Journal : Ebj |
| Vaitiekunas P, Crane-Robinson C, Privalov PL. (2015) The energetic basis of the DNA double helix: a combined microcalorimetric approach. Nucleic Acids Research. 43: 8577-89 |
| Tiktopulo EI, Privalov PL. (2015) Heat denaturation of ribonuclease. Biophysical Chemistry. 1: 349-57 |
| Shukla H, Vaitiekunas P, Majumdar AK, et al. (2012) The linker of the interferon response factor 3 transcription factor is not unfolded Biochemistry. 51: 6320-6327 |
| Privalov PL, Dragan AI, Crane-Robinson C. (2011) Interpreting protein/DNA interactions: Distinguishing specific from non-specific and electrostatic from non-electrostatic components Nucleic Acids Research. 39: 2483-2491 |
| Carrillo RJ, Privalov PL. (2010) Unfolding of bZIP dimers formed by the ATF-2 and c-Jun transcription factors is not a simple two-state transition. Biophysical Chemistry. 151: 149-54 |