Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy.
about
Crystal structures of myoglobin-ligand complexes at near-atomic resolution.Conformational substates and motions in myoglobin. External influences on structure and dynamics.Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobinProtein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes.Time-resolved visible and infrared study of the cyano complexes of myoglobin and of hemoglobin I from Lucina pectinata.Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin.Probing anisotropic structure changes in proteins with picosecond time-resolved small-angle X-ray scattering.Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobin.Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin.Ultrafast infrared spectroscopy of bacteriorhodopsin.Theory of photoselection by intense light pulses. Influence of reorientational dynamics and chemical kinetics on absorbance measurements.Photoselection in polarized photolysis experiments on heme proteinsMolecular dynamics simulations of heme reorientational motions in myoglobin.Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneityDirect observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopyDirect measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomeraseApplications of ultrafast laser spectroscopy for the study of biological systems.Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kineticsPicosecond infrared studies of the dynamics of the photosynthetic reaction centerThe effects of heme pocket hydrophobicity on the ligand binding dynamics in myoglobin as studied with leucine 29 mutants.Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.Electronic structure of ions and molecules in solution: a view from modern soft X-ray spectroscopies.Distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of three distal mutants.Modelling multi-pulse population dynamics from ultrafast spectroscopy.The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers.CO rebinding to protoheme: investigations of the proximal and distal contributions to the geminate rebinding barrierEquilibrium versus Nonequilibrium Peptide Dynamics: Insights into Transient 2D IR Spectroscopy
P2860
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P2860
Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy.
description
1988 nî lūn-bûn
@nan
1988 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
name
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@ast
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@en
type
label
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@ast
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@en
prefLabel
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@ast
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@en
P2093
P2860
P356
P1476
Iron-carbonyl bond geometries ...... esolved infrared spectroscopy.
@en
P2093
P A Hansen
R M Hochstrasser
P2860
P304
P356
10.1073/PNAS.85.14.5062
P407
P577
1988-07-01T00:00:00Z