Conformational change of proteins arising from normal mode calculations.
By F. Tama, Yves-Henri Sanejouand. Protein Engineering, 2001
874 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/3b6ea57bb0f0378608965458c5ec50405ced105a
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In Materials Chemistry
- Ivet Bahar
- Marc Delarue
- A. Rader
- Erik Lindahl
- Patrice Koehl
- Cyril Azuara
- José Ramón López-Blanco
- Pablo Chacón
In Molecular Biology
- Ivet Bahar
- Nelly Andrusier
- Efrat Mashiach
- Haim J. Wolfson
- Marc Delarue
- Ruth Nussinov
- A. Rader
- Erik Lindahl
Citations in the corpus
- Impact of protein conformational diversity on AlphaFold predictions (2021, methodology): “We perform the NMA for the apo form of the protein on the basis that normal modes obtained with the apo form of a given protein give a better description of the conformational change than those obtained with the holo form [53] .”
- Evolutionary Conserved Positions Define Protein Conformational Diversity (2016, background): “A number of studies applied on vastly different enzymes show that conformational transitions are dominated by only a few low-frequency normal modes[35,46,47].”
- ElNémo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement (2004, background): “Moreover, when the collective character of the protein motion is obvious, a single lowfrequency normal mode often proves to be enough, and it is usually one of the three lowest-frequency ones (12,13).”
- Coarse-grained normal mode analysis in structural biology. (2005, background): “The free energy changes associated with H/D exchange of individual amino acids measured near native state conditions for a series of proteins have been correlated, for example, with the entropic costs predicted by the GNM [54]; the experimentally observed structural changes of enzymes between their ”
- NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis (2006, background): “The server provides functionality to calculate ‘overlap coefficients’ (scalar products) between the coordinate difference vectors of two superimposed structures and the eigenvectors of the 100 lowest frequency normal modes (23).”
- Simplified normal mode analysis of conformational transitions in DNA-dependent polymerases: the elastic network model. (2002, methodology): “The index of collectiveness of each mode was defined and calculated as described.(47) All programs used here are available upon request (sanejouand@crpp.”
- iMod: multipurpose normal mode analysis in internal coordinates (2011, positive): “It is well known that NMA performs better from open forms (Tama and Sanejouand, 2001).”
- Principles of Flexible Protein-Protein Docking (2008, background): “It has been shown43,44 that the first few normal modes, with the lowest frequencies, can describe much of a conformational change.”