The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.

The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.

Item
http://www.wikidata.org/entity/Q46696953
Subunit-selective interrogation of CO recombination in carbonmonoxy hemoglobin by isotope-edited time-resolved resonance Raman spectroscopyOptical Detection of Disordered Water within a Protein CavityImaging the migration pathways for O2, CO, NO, and Xe inside myoglobin.Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.Glass matrix-facilitated thermal reduction: a tool for probing reactions of met hemoglobin with nitrite and nitric oxide.Recombinant hemoglobin II from Lucina pectinata: a large-scale method for hemeprotein expression in E. coliWater and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation.Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Ligand recombination and a hierarchy of solvent slaved dynamics: the origin of kinetic phases in hemeproteins.O2 migration pathways are not conserved across proteins of a similar fold.Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation.Effects of active site mutations in haemoglobin I from Lucina pectinata: a molecular dynamic study.Reactivity of glass-embedded met hemoglobin derivatives toward external NO: implications for nitrite-mediated production of bioactive NO.Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.Dynamics of nitric oxide rebinding and escape in horseradish peroxidase.Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structure.
P2860

The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities.

Item
http://www.wikidata.org/entity/Q46696953
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
The position 68(E11) side chai ...... ement into the xenon cavities.
@en
The position 68(E11) side chai ...... ement into the xenon cavities.
@nl
type
label
The position 68(E11) side chai ...... ement into the xenon cavities.
@en
The position 68(E11) side chai ...... ement into the xenon cavities.
@nl
prefLabel
The position 68(E11) side chai ...... ement into the xenon cavities.
@en
The position 68(E11) side chai ...... ement into the xenon cavities.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
The position 68(E11) side chai ...... ement into the xenon cavities.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698