about
CHARMM: the biomolecular simulation programReverse engineering the cooperative machinery of human hemoglobinIn crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0Metal Ion Modeling Using Classical MechanicsModel compounds for the T state of hemoglobinHow many base-pairs per turn does DNA have in solution and in chromatin? Some theoretical calculationsA new mode for heme-heme interactions in hemoglobin associated with distal perturbations.Conformational kinetics of triligated hemoglobinEnergetics of enzyme catalysis.Semiempirical calculations of model deoxyheme. Variation of calculated electromagnetic properties with electronic configuration and distance of iron from the plane.An abasic site in DNA. Solution conformation determined by proton NMR and molecular mechanics calculations.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitationA quantum-chemical picture of hemoglobin affinityProbing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin.Steric control of CO binding in a totally synthetic heme protein modelProtein dynamics explain the allosteric behaviors of hemoglobin.Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.Coupling between oxidation state and hydrogen bond conformation in heme proteins.Structure-specific model of hemoglobin cooperativity.Charge stabilization mechanism in the visual and purple membrane pigments.Allosteric linkage-induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering.Detection of the heme perturbations caused by the quaternary R----T transition in oxyhemoglobin trout IV by resonance Raman scatteringTertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.Multiphoton absorption of myoglobin-nitric oxide complex: relaxation by D-NEMD of a stationary state.Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect.Geometry of intercalation of psoralens in DNA approached by molecular mechanics.The binding characteristics of the cytochrome c iron.Direct evidence for mode-specific vibrational energy relaxation from quantum time-dependent perturbation theory. I. Five-coordinate ferrous iron porphyrin model.Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size
P2860
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P2860
description
1977 nî lūn-bûn
@nan
1977 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի մարտին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年論文
@yue
1977年論文
@zh-hant
1977年論文
@zh-hk
1977年論文
@zh-mo
1977年論文
@zh-tw
1977年论文
@wuu
name
Mechanism of tertiary structural change in hemoglobin.
@ast
Mechanism of tertiary structural change in hemoglobin.
@en
type
label
Mechanism of tertiary structural change in hemoglobin.
@ast
Mechanism of tertiary structural change in hemoglobin.
@en
prefLabel
Mechanism of tertiary structural change in hemoglobin.
@ast
Mechanism of tertiary structural change in hemoglobin.
@en
P2860
P356
P1476
Mechanism of tertiary structural change in hemoglobin.
@en
P2093
P2860
P304
P356
10.1073/PNAS.74.3.801
P407
P577
1977-03-01T00:00:00Z