Anchor profiles of HLA‐specific peptides: Analysis by a novel affinity scoring method and experimental validation

Anchor profiles of HLA‐specific peptides: Analysis by a novel affinity scoring method and experimental validation

Source :

• Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 2005-01-01.

English descriptors

• Teeft :
  • Absolute value, Acid residues, Acid substitutions, Algorithm, Aliphatic, Aliphatic moiety, Aliphatic residues, Amide, Amide group, Amino, Amino acid, Amino acid model compounds, Amino acid side chains, Amino acids, Anchor, Anchor position, Anchor positions, Anchor preferences, Anchor profiles, Anchor residues, Anchor substitutions, Anking peptide groups, Aromatic, Aromatic groups, Assay, Bimas, Bimas matrix, Bimas score syfpeithi score, Binding, Binding capacities, Binding capacity, Binding energy, Binding groove, Binding peptides, Biol, Carboxylate groups, Charmm, Chemical group, Complex formation, Complex models, Conformation, Conformational, Conformational space, Conformational strain, Conjugate gradient minimization, Correlation plot, Curr opin struct biol, Cutoff, Data sets, Delicate balance, Descent energy minimization, Desmet, Desolvation, Desolvation effects, Desolvation energies, Desolvation energy, Desolvation term, Desolvation terms, Direct comparison, Direct interactions, Docking, Docking algorithm, Electrostatic energy, Electrostatic interactions, Energetic analysis, Energetic cost, Energy functions, Energy score, Entropic effects, Exible, Exible peptides, Experimental data, Experimental information, Experimental validation, Experimental values, Explicit water molecules, Flexible docking, Flskqymtl, Free energies, Free energy, Free energy calculations, Free energy perturbation, Gexp score, Guanidinium, Guanidinium group, Guanidinium groups, Histocompatibility, Hydration, Hydration energies, Hydration energy, Hydrophobic, Immunol, Interaction, Interaction energy, Intermolecular interactions, Intracomplex, Intracomplex energies, Intracomplex interactions, Intracomplex terms, Kluwer press, Ligand, Ligand binding, Local interactions, Logkd, Main purpose, Major histocompatibility, Matrix, Minimization, Model preparation step, Modeling, Moiety, Molecule, Multiple representations, Mutant, Mutation, Nonanchor residues, Nonbonded interactions, Other residue types, Pepscope, Pepscope method, Pepscope score sidney, Peptide, Peptide backbone, Peptide binding, Peptide flskqymtl, Peptide ligands, Peptide motifs, Peptide sequence, Peptide sequences, Peptides table, Possible explanation, Prediction, Prediction accuracy, Prediction methods, Prediction scores, Preferred residues, Primary reason, Proc natl acad, Prohibitive nature, Protein data bank, Rational drug design, Receptor, Receptor complexes, Receptor type, Reference peptide, Regression line, Residue, Residue types, Rotamer, Rotamer library, Rotameric, Rotameric sampling, Same approach, Same charmm force, Second group, Secondary anchor residues, Self energy, Sette, Simulation, Smaller ones, Solvation, Solvent model, Solvent terms, Solvent water, Standard geometry, Strain contributions, Strain terms, Striking observation, Strong binding, Strong interactions, Strong preference, Structural data, Substitution, Syfpeithi, Systematic errors, Test peptide, Total energy, Total scores, Transferability, Uncalibrated score, Validation, Validation experiments, Waals, Waals interactions, Waals parameters, Water molecules.

Abstract

• https://api.istex.fr/ark:/67375/WNG-ZP921NZL-6/fulltext.pdf

Affiliations:

• Belgique

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