Folding a protein in a computer: An atomic description of the folding/unfolding of protein A
By A. Garcia, José N. Onuchic. Proceedings of the National Academy of Sciences of the United States of America, 2003
305 citations recorded by the source corpus.
Subfields: Atomic and Molecular Physics, and Optics, Materials Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b224200efc21cfb6d7c373d22a2cba932c335286
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In Atomic and Molecular Physics, and Optics
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Citations in the corpus
- Enhanced Sampling in Molecular Dynamics Using Metadynamics, Replica-Exchange, and Temperature-Acceleration (2013, background): “Parallel tempering is popular in simulations of protein conformational sampling [197,198], protein folding [189,199–203] and aggregation [204,205], due at least in part to the fact that one need not choose CVs to use it, and CVs for describing these processes are not always straightforward to determ”
- Water mediation in protein folding and molecular recognition. (2006, methodology): “Moreover, these fully atomistic simulations (57, 119, 132, 133), which are not biased toward direct contacts between the residues, point out that the folded state is not completely dry but that a few core water molecules form hydrogen bonds with the protein backbone.”
- The protein folding 'speed limit'. (2004, unknown): “3 310 [127] [91,119,128–146]”