Simultaneous determination of protein structure and dynamics

By K. Lindorff‐Larsen, Robert B. Best, Mark A. DePristo, Christopher M. Dobson, Michele Vendruscolo. Nature, 2005

683 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/98db8dbe29d3dc660be34aa6fdeb0316ea035f84

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Citations in the corpus

Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints (2008, background): “For a case such as MSG, which is characterized by a very low density of experimental restraints, such treatment is not recommended unless the individual domains are held rigidly and/or additional restraints such as order parameters are used to limit the spread of the structural ensemble (Lindorff-La”
Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin (2006, background): “Recent work relating the structure and dynamics of human ubiquitin has predicted an unprecedented diversity in the conformations of the native-state ensembl”
Accurate Structural Correlations from Maximum Likelihood Superpositions (2008, methodology): “For instance, Figure 5A and 5C shows the largest principal mode of correlation from solution structures of ubiquitin solved by dynamic ensemble refinement, which takes into account the dynamic heterogeneity of a protein as measured by NMR relaxation experiments in addition to NOE distance constraint”
Developing a molecular dynamics force field for both folded and disordered protein states (2018, methodology): “RDCs of folded proteins were calculated as reported previously (60).”
Assessment of protein structure refinement in CASP9 (2011, methodology): “We have followed a similar procedure as in the last CASP1 by comparing to either the nuclear magnetic resonance (NMR) information coming from nuclear Overhauser effect (NOE) data31,32 or by doing MR likelihood analysis24,25 on X-ray structures.”
Assessment of the protein-structure refinement category in CASP8 (2009, background): “31,32 This procedure is attractive because of its relative simplicity.”