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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

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Reference TypeJournal (article/letter/editorial)
TitleStructural Dynamics of the Potassium Channel Blocker ShK: SRLS Analysis of 15N Relaxation
JournalThe Journal of Physical Chemistry B
AuthorsMeirovitch, EvaAuthor
Tchaicheeyan, OrenAuthor
Sher, InbalAuthor
Norton, Raymond S.Author
Chill, Jordan H.Author
Year2015 (December 10)Volume119
Issue49
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/acs.jpcb.5b07875Search in ResearchGate
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Mindat Ref. ID3885890Long-form Identifiermindat:1:5:3885890:9
GUID0
Full ReferenceMeirovitch, 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
Plain TextMeirovitch, 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
In(2015, December) The Journal of Physical Chemistry B Vol. 119 (49) American Chemical Society (ACS)

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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 PLCγ1C SH2. The Journal of Physical Chemistry B, 120 (41). 10695-10705 doi:10.1021/acs.jpcb.6b08264
Mendelman, Netanel, Meirovitch, Eva (2021) Structural Dynamics from NMR Relaxation by SRLS Analysis: Local Geometry, Potential Energy Landscapes, and Spectral Densities. The Journal of Physical Chemistry B, 125 (23) 6130-6143 doi:10.1021/acs.jpcb.1c02502
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, 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, 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
Mendelman, Netanel, Meirovitch, Eva (2021) SRLS Analysis of 15N–1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy. The Journal of Physical Chemistry B, 125 (3) 805-816 doi:10.1021/acs.jpcb.0c10124
Shapiro, Yury E., Meirovitch, Eva (2012) Slowly Relaxing Local Structure (SRLS) Analysis of 15N–H Relaxation from the Prototypical Small Proteins GB1 and GB3. The Journal of Physical Chemistry B, 116 (13). 4056-4068 doi:10.1021/jp300245k
Meirovitch, Eva, Shapiro, Yury E., Zerbetto, Mirco, Polimeno, Antonino (2012) SRLS Analysis of 15N Spin Relaxation from E. coli Ribonuclease HI: The Tensorial Perspective. The Journal of Physical Chemistry B, 116 (2). 886-894 doi:10.1021/jp208767s
Zerbetto, Mirco, Meirovitch, Eva (2017) 15N–H-Related Conformational Entropy Changes Entailed By Plexin-B1 RBD Dimerization: Combined Molecular Dynamics/NMR Relaxation Approach. The Journal of Physical Chemistry B, 121 (14). 3007-3015 doi:10.1021/acs.jpcb.7b01079
Meirovitch, Eva (2012) SRLS Analysis of15N Relaxation from Bacteriophage T4 Lysozyme: a Tensorial Perspective That Features Domain Motion. The Journal of Physical Chemistry B, 116 (21). 6118-6127 doi:10.1021/jp301999n
 
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