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Tchaicheeyan, Oren, Freed, Jack H., Meirovitch, Eva (2016) Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry. The Journal of Physical Chemistry B, 120 (11). 2886-2898 doi:10.1021/acs.jpcb.6b00524

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Reference TypeJournal (article/letter/editorial)
TitleLocal Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry
JournalThe Journal of Physical Chemistry B
AuthorsTchaicheeyan, OrenAuthor
Freed, Jack H.Author
Meirovitch, EvaAuthor
Year2016 (March 24)Volume120
Issue11
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/acs.jpcb.6b00524Search in ResearchGate
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Mindat Ref. ID3886263Long-form Identifiermindat:1:5:3886263:8
GUID0
Full ReferenceTchaicheeyan, Oren, Freed, Jack H., Meirovitch, Eva (2016) Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry. The Journal of Physical Chemistry B, 120 (11). 2886-2898 doi:10.1021/acs.jpcb.6b00524
Plain TextTchaicheeyan, Oren, Freed, Jack H., Meirovitch, Eva (2016) Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry. The Journal of Physical Chemistry B, 120 (11). 2886-2898 doi:10.1021/acs.jpcb.6b00524
In(2016, March) The Journal of Physical Chemistry B Vol. 120 (11) American Chemical Society (ACS)

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Tchaicheeyan, Oren, Mendelman, Netanel, Zerbetto, Mirco, Meirovitch, Eva (2019) Local Ordering at Mobile Sites in Proteins: Combining Perspectives from NMR Relaxation and Molecular Dynamics. The Journal of Physical Chemistry B, 123 (13). 2745-2755 doi:10.1021/acs.jpcb.8b10801
Tchaicheeyan, Oren, Meirovitch, Eva (2016) Polar Versus Non-polar Local Ordering at Mobile Sites in Proteins: Slowly Relaxing Local Structure Analysis of 15N Relaxation in the Third Immunoglobulin-Binding Domain of Streptococcal Protein G. The Journal of Physical Chemistry B, 120 (3). 386-395 doi:10.1021/acs.jpcb.5b10244
Tchaicheeyan, Oren, Meirovitch, Eva (2017) Conformational Entropy from NMR Relaxation in Proteins: The SRLS Perspective. The Journal of Physical Chemistry B, 121 (4). 758-768 doi:10.1021/acs.jpcb.6b13034
Tchaicheeyan, Oren, Meirovitch, Eva (2016) An SRLS Study of 2H Methyl-Moiety Relaxation and Related Conformational Entropy in Free and Peptide-Bound PLCÎł1C SH2. The Journal of Physical Chemistry B, 120 (41). 10695-10705 doi:10.1021/acs.jpcb.6b08264
Meirovitch, Eva, Polimeno, Antonino, Freed, Jack H. (2006) Methyl Dynamics in Proteins from NMR Slowly Relaxing Local Structure Spin Relaxation Analysis:  A New Perspective. The Journal of Physical Chemistry B, 110 (41). 20615-20628 doi:10.1021/jp061403+
Meirovitch, Eva, Shapiro, Yury E., Polimeno, Antonino, Freed, Jack H. (2007) An Improved Picture of Methyl Dynamics in Proteins from Slowly Relaxing Local Structure Analysis of2H Spin Relaxation. The Journal of Physical Chemistry B, 111 (44). 12865-12875 doi:10.1021/jp072156s
Meirovitch, Eva, Tchaicheeyan, Oren, Sher, Inbal, Norton, Raymond S., Chill, Jordan H. (2015) Structural Dynamics of the Potassium Channel Blocker ShK: SRLS Analysis of 15N Relaxation. The Journal of Physical Chemistry B, 119 (49). 15130-15137 doi:10.1021/acs.jpcb.5b07875
Mendelman, Netanel, Meirovitch, Eva (2020) Conformational Entropy from Restricted Bond-Vector Motion in Proteins: The Symmetry of the Local Restrictions and Relation to NMR Relaxation. The Journal of Physical Chemistry B, 124 (21) 4284-4292 doi:10.1021/acs.jpcb.0c02662
Meirovitch, Eva, Liang, Zhichun, Freed, Jack H. (2018) Phenyl-Ring Dynamics in Amyloid Fibrils and Proteins: The Microscopic-Order-Macroscopic-Disorder Perspective. The Journal of Physical Chemistry B, 122 (37). 8675-8684 doi:10.1021/acs.jpcb.8b06330
Pshetitsky, Yaron, Buck, Matthias, Meirovitch, Eva (2024) Local Structures in Proteins from Microsecond Molecular Dynamics Simulations: 2. The Role of Symmetry in GTPase Binding and Dimer Formation. The Journal of Physical Chemistry B, 128 (7) 1573-1585 doi:10.1021/acs.jpcb.3c06745
Meirovitch, Eva, Dzikovski, Boris, Freed, Jack H. (2019) Comment on “Distinct Populations in Spin-Label EPR Spectra from Nitroxides”. The Journal of Physical Chemistry B, 123 (10). 2454-2456 doi:10.1021/acs.jpcb.8b07730
 
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