2025
Relationship between immunogenicity and protein structure at amino acid substitution sites of blood group antigens
Howe J, Stack G. Relationship between immunogenicity and protein structure at amino acid substitution sites of blood group antigens. Blood 2025, 146: 504-517. PMID: 40163810, DOI: 10.1182/blood.2024025071.Peer-Reviewed Original ResearchProtein structureAa substitutionsBlood group antigensThree-dimensional protein structuresAmino acid substitution sitesAmino acidsGroup antigensSurface-accessible loopsInvestigating protein structureStructure predictionProtein regionsB strandsTertiary structureFlexible regionsInformatics analysisAlphaFold2ProteinAminoImmunogenic antigensSitesDeterminants of immunogenicitySubstitutionPolypeptideConfidence scoresDisordered coils
2009
Allostery and conformational free energy changes in human tryptophanyl‐tRNA synthetase from essential dynamics and structure networks
Bhattacharyya M, Ghosh A, Hansia P, Vishveshwara S. Allostery and conformational free energy changes in human tryptophanyl‐tRNA synthetase from essential dynamics and structure networks. Proteins Structure Function And Bioinformatics 2009, 78: 506-517. PMID: 19768679, DOI: 10.1002/prot.22573.Peer-Reviewed Original ResearchConceptsHuman tryptophanyl-tRNA synthetaseTryptophanyl-tRNA synthetaseConcept of allosteryProtein structure networksProtein complexesMultidomain proteinsAllosteric communicationFunctional insightsProtein biosynthesisCognate tRNAAllosteric mechanismAllosteryConformational free energy changesEnzymatic catalysisConformational mobilityFlexible regionsMolecular levelAmino acidsProteinStructure networkMolecular-level understandingFree energy landscapePopulation shiftsMolecular dynamics simulationsFree energy change
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