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Rotamer libraries in the 21st century
scientific article (publication date: August 2002)
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scholarly article
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review article
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Europe PubMed Central
title
Rotamer libraries in the 21st century
(English)
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main subject
rotamer
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author
Roland Dunbrack
series ordinal
1
object named as
Roland L Dunbrack
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language of work or name
English
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publication date
August 2002
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published in
Current Opinion in Structural Biology
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volume
12
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issue
4
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page(s)
431-40
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cites work
An analysis of side-chain conformation in proteins
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Conformation of amino acid side-chains in proteins
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Structure and refinement of penicillopepsin at 1.8 Å resolution
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Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
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Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
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A new approach to the rapid determination of protein side chain conformations
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Backbone-dependent rotamer library for proteins. Application to side-chain prediction
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Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins.
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All in one: a highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end elimination
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Bayesian statistical analysis of protein side-chain rotamer preferences
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The penultimate rotamer library
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Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms
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Asparagine and glutamine rotamers: B-factor cutoff and correction of amide flips yield distinct clustering
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Protein sidechain conformer prediction: a test of the energy function
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Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains
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Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment
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An atoms-in-molecules study of the genetically-encoded amino acids: I. Effects of conformation and of tautomerization on geometric, atomic, and bond properties
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A statistical analysis of side-chain conformations in proteins: comparison with ECEPP predictions
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Studies on the conformation of amino acids. IX. Conformations of butyl, seryl, threonyl, cysteinyl, and valyl residues in a dipeptide unit
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The interrelationships of side-chain and main-chain conformations in proteins.
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Main-chain conformational features at different conformations of the side-chains in proteins.
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Protein side-chain conformation: a systematic variation of chi 1 mean values with resolution - a consequence of multiple rotameric states?
1 reference
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Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences
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Analysis of a data set of paired uncomplexed protein structures: new metrics for side-chain flexibility and model evaluation.
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Side-chain flexibility in proteins upon ligand binding.
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Rotamer strain energy in protein helices - quantification of a major force opposing protein folding
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Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core
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The energetics of off-rotamer protein side-chain conformations
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Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
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Hydrogen bonds between short polar side chains and peptide backbone: prevalence in proteins and effects on helix-forming propensities
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Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid.
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Prediction of protein side-chain rotamers from a backbone-dependent rotamer library: a new homology modeling tool
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7 January 2021
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1 reference
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7 January 2021
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7 January 2021
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1 reference
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Identifiers
DOI
10.1016/S0959-440X(02)00344-5
1 reference
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Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2796799
Fatcat ID
release_brh6456wl5gqphepnue6unucra
1 reference
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OpenCitations bibliographic resource ID
2796799
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2796799
PubMed publication ID
12163064
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2796799
ResearchGate publication ID
11223819
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