Proteins: Structures and Molecular Properties

By T. Creighton. 1986

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Citations in the corpus

Evaluating Protein Transfer Learning with TAPE (2019, background): “Though structure is constrained by evolutionary pressures, sequence-level variation can be high, with very different sequences having similar structure [18].”
Classification of Intrinsically Disordered Regions and Proteins (2014, unknown): “347,348 The presence of hydrophobic surface residues, for example, binding sites for other proteins, and the denaturation of otherwise folded proteins lead to the exposure of hydrophobic residues to water and reduce solubility, sometimes leading to aggregation and precipitation.”
Extending the treatment of backbone energetics in protein force fields: Limitations of gas‐phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations (2004, background): “63 In all four maps the C5 region is similar, being relatively ﬂat.”
EigenTHREADER: analogous protein fold recognition by efficient contact map threading (2017, background): “Indeed, this insight is the basis of solving protein structures by NMR data (Creighton, 1992).”
Protein secondary structure: category assignment and predictability (2001, background): “The energy stored in a good hydrogen bond is approximately 2 kcal/ mol, exceeding by a factor of 10 the van der Waals energy [5], which means that the energies stored in To investigate characteristics at hydrogen bond interactions are dominant at the secondary structure level, except for S^S…”
Atomic Biology, Electrostatics, and Ionic Channels (2008, background): “And that certainly seems, at first blush, to be enough to calculate the short range interactions in a system.”
Missense meanderings in sequence space: a biophysical view of protein evolution (2005, background): “To put these values in context, the energy of a single hydrogen bond is 2–10 kcal mol −1 (Ref”