Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
about
The crystal structure of a tetrameric hemoglobin in a partial hemichrome stateLigand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.Characterization of the myoglobin and its coding gene of the mollusc Biomphalaria glabrata.The molecular basis of high-altitude adaptation in deer mice.Molecular controls of the oxygenation and redox reactions of hemoglobinPolymerization of hemoglobins in Arctic fish: Lycodes reticulatus and Gadus morhua.Expression of fully functional tetrameric human hemoglobin in Escherichia coliResonance Raman enhancement of phenyl ring vibrational modes in phenyl iron complex of myoglobin.Ligand binding to heme proteins. V. Light-induced relaxation in proximal mutants L89I and H97F of carbonmonoxymyoglobin.The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor.How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase.Extracting protein alignment models from the sequence database.Mutational studies of protein structures and their stabilities.New look at hemoglobin allostery.Transmembrane heme delivery systems.Primary structure of a dimeric haemoglobin from the deep-sea cold-seep clam Calyptogena soyoaeApplication of molecular dynamics and free energy perturbation methods to metalloporphyrin-ligand systems II: CO and dioxygen binding to myoglobinAdaptive functional divergence among triplicated alpha-globin genes in rodentsCrystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocketCoexpression of human alpha- and circularly permuted beta-globins yields a hemoglobin with normal R state but modified T state propertiesVariations on the theme: allosteric control in hemoglobin.Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin.Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study.Polymerization and solubility of recombinant hemoglobins alpha 2 beta 2 (6Val) (Hb S) and alpha 2 beta 2(6Leu) (Hb Leu).LZnX complexes of tripodal ligands with intramolecular RN-H hydrogen bonding groups: structural implications of a hydrogen bonding cavity, and of X/R in the hydrogen bonding geometry/strength.The oxygen transport system in three species of the boreal fish family Gadidae. Molecular phylogeny of hemoglobin.Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N-H Acidity of the Distal Base.A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins.Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.Site-directed mutagenesis in hemoglobinRelative importance of hydrogen bonding and coordinating groups in modulating the zinc–water acidity
P2860
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P2860
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
description
1987 nî lūn-bûn
@nan
1987 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@ast
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@en
type
label
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@ast
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@en
prefLabel
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@ast
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@en
P2093
P356
P1433
P1476
Distal residues in the oxygen binding site of haemoglobin studied by protein engineering.
@en
P2093
De Young A
Kwiatkowsky L
Miyazaki G
P2888
P304
P356
10.1038/329858A0
P407
P577
1987-10-01T00:00:00Z
P6179
1047648033