Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds.
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How are model protein structures distributed in sequence space?Statistical potential for assessment and prediction of protein structuresRecognizing misfolded and distorted protein structures by the assumption-based similarity score.How to generate improved potentials for protein tertiary structure prediction: a lattice model study.Statistical potentials for fold assessment.Information-theoretic dissection of pairwise contact potentials.Propensity scores for prediction and characterization of bioluminescent proteins from sequences.Polar profile of antiviral peptides from AVPpred Database.Residue contact-count potentials are as effective as residue-residue contact-type potentials for ranking protein decoys.Splitting statistical potentials into meaningful scoring functions: testing the prediction of near-native structures from decoy conformations.Information-theoretic analysis of the reference state in contact potentials used for protein structure prediction.Discrimination of Native-like States of Membrane Proteins with Implicit Membrane-based Scoring Functions.LoCo: a novel main chain scoring function for protein structure prediction based on local coordinatesA position-specific distance-dependent statistical potential for protein structure and functional studySelf-consistently optimized energy functions for protein structure prediction by molecular dynamics.A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.Discriminating the native structure from decoys using scoring functions based on the residue packing in globular proteins.From isotropic to anisotropic side chain representations: comparison of three models for residue contact estimationThe dependence of all-atom statistical potentials on structural training database.Atom depth as a descriptor of the protein interior.An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure.Mapping hydrophobicity on the protein molecular surface at atom-level resolution.Three-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel foldA novel index of protein-protein interface propensity improves interface residue recognitionA preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor designIdeal architecture of residue packing and its observation in protein structures.Identification of cooperative folding units in a set of native proteinsConcepts in protein folding.Reduced C(beta) statistical potentials can outperform all-atom potentials in decoy identification.An iterative method for extracting energy-like quantities from protein structures.Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination.Hydrophobicity--shake flasks, protein folding and drug discovery.Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction.How do side chains orient globally in protein structures?Towards protein folding by global energy optimization.50 years of amino acid hydrophobicity scales: revisiting the capacity for peptide classification.Predicting the helix packing of globular proteins by self-correcting distance geometryHydrophobic regions on protein surfaces. Derivation of the solvation energy from their area distribution in crystallographic protein structures.Propensities, probabilities, and the Boltzmann hypothesis.Orientation-dependent potential of mean force for protein folding.
P2860
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P2860
Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Structure-derived hydrophobic ...... able to identify native folds.
@ast
Structure-derived hydrophobic ...... able to identify native folds.
@en
type
label
Structure-derived hydrophobic ...... able to identify native folds.
@ast
Structure-derived hydrophobic ...... able to identify native folds.
@en
prefLabel
Structure-derived hydrophobic ...... able to identify native folds.
@ast
Structure-derived hydrophobic ...... able to identify native folds.
@en
P1476
Structure-derived hydrophobic ...... able to identify native folds.
@en
P2093
P304
P356
10.1016/0022-2836(92)90556-Y
P407
P577
1992-04-01T00:00:00Z