Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations
Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations(804 views) Langella E, Improta R, Crescenzi O, Barone V
Keywords: Conformational Transition, Electrostatic Calculation, Histidine Titration, Molecular Dynamics, Pkα, Prion Protein, Acid Base Balance, Article, Carboxy Terminal Sequence, Human, Molecular Model, Priority Journal, Protein Conformation, Protein Domain, Protein Structure, Proton Transport, Simulation, Titrimetry, Amino Acid Sequence, Computer Simulation, Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy, Peptide Fragments,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Universitá Federico II, Complesso di Monte S. Angelo, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
References: Not available.
Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations
Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations
Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations