[NMR paper] A Free-Energy Landscape Analysis of Calmodulin Obtained from an NMR Data-Utilized Multi-Scale Divide-and-Conquer Molecular Dynamics Simulation
Calmodulin (CaM) is a multifunctional calcium-binding protein, which regulates a variety of biochemical processes. CaM acts through its conformational changes and complex formation with its target enzymes. CaM consists of two globular domains (N-lobe and C-lobe) linked by an extended linker region. Upon calcium binding, the N-lobe and C-lobe undergo local conformational changes, followed by a major conformational change of the entire CaM to wrap the target enzyme. However, the regulation...
[NMR paper] Mapping the energy landscape of protein-ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion
Mapping the energy landscape of protein-ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion
Biochemical signaling is mediated by complexes between macromolecular receptors and their ligands, with the duration of the signal being directly related to the lifetime of the ligand-receptor complex. In the field of drug design, the recognition that drug efficacy in vivo depends on the lifetime of the drug-protein complex has spawned the concept of designing drugs with particular binding kinetics. To advance this field it is critical to investigate...
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08-31-2021 10:53 AM
Characterization of Protein Kinase a Free Energy Landscape by NMR-Restrained Metadynamics
Characterization of Protein Kinase a Free Energy Landscape by NMR-Restrained Metadynamics
Publication date: 3 February 2017
Source:Biophysical Journal, Volume 112, Issue 3, Supplement 1</br>
Author(s): Yingjie Wang, Carlo Camilloni, Jonggul Kim, Michele Vendruscolo, Jiali Gao, Gianluigi Veglia</br>
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02-03-2017 09:55 PM
[NMR paper] Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Phys Chem Chem Phys. 2017 Jan 09;:
Authors: Borkar AN, Vallurupalli P, Camilloni C, Kay LE, Vendruscolo M
Abstract
RNA molecules in solution tend to undergo structural fluctuations of...
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01-12-2017 03:48 AM
[NMR paper] Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
Related Articles Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
J Phys Chem Lett. 2016 Jun 14;
Authors: Salvi N, Abyzov A, Blackledge M
Abstract
Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their functional states. Although this plasticity is essential to their function, little is known about the dynamics underlying...
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06-15-2016 11:12 PM
Variability and conservation of structural domains in divide-and-conquer approaches
Variability and conservation of structural domains in divide-and-conquer approaches
Abstract
The use of protein building blocks for the structure determination of multidomain proteins and proteinâ??protein complexes, also known as the â??divide and conquerâ?? approach, is an important strategy for obtaining protein structures. Atomic-resolution X-ray or NMR data of the individual domains are combined with lower-resolution electron microscopy maps or X-ray data of the full-length protein or the protein complex. Doing so, it is often assumed that the...
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05-30-2016 01:15 PM
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
Celia Sanchez-Medina, Ashok Sekhar, Pramodh Vallurupalli, Michele Cerminara, Victor Mun?oz and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja502705y/aop/images/medium/ja-2014-02705y_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja502705y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
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[NMR paper] The pressure-temperature free energy-landscape of staphylococcal nuclease monitored b
The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
Related Articles The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
J Mol Biol. 2000 Apr 28;298(2):293-302
Authors: Lassalle MW, Yamada H, Akasaka K
The thermodynamic stability of staphylococcal nuclease was studied against the variation of both temperature and pressure by utilizing (1)H NMR spectroscopy at 750 MHz in 20 mM Mes buffer containing 99.9 % (2)H(2)O, pH 5.3. Equilibrium fractions of folded...
A Free-Energy Landscape Analysis of Calmodulin Obtained from an NMR Data-Utilized Multi-Scale Divide-and-Conquer Molecular Dynamics Simulation
Linear Mode
