Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
about
The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homologStructural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand TransportLigand-induced conformational changes in a thermophilic ribose-binding proteinStructural Analysis of Semi-specific Oligosaccharide Recognition by a Cellulose-binding Protein of Thermotoga maritima Reveals Adaptations for Functional Diversification of the Oligopeptide Periplasmic Binding Protein FoldThe structural basis for partitioning of the XRCC1/DNA ligase III- BRCT-mediated dimer complexesMolecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding proteinMutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome cDenaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfoldingA polar, solvent-exposed residue can be essential for native protein structureEffect of sequential deletion of extra N-terminal residues on the structure and stability of yeast iso-1-cytochrome-c.Baseline length and automated fitting of denaturation data.Duplication of genes in an ATP-binding cassette transport system increases dynamic range while maintaining ligand specificity.Thermal denaturation of iso-1-cytochrome c variants: comparison with solvent denaturation.Thermal stability of hydrophobic heme pocket variants of oxidized cytochrome cRequirements for perpendicular helix pairing.Effect of an Ala81His mutation on the Met80 loop dynamics of iso-1-cytochrome c.Overexpression, purification, and enthalpy of unfolding of ferricytochrome c552 from a psychrophilic microorganism.Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c.A Structural Study of CESA1 Catalytic Domain of Arabidopsis Cellulose Synthesis Complex: Evidence for CESA Trimers.Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins.Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility
P2860
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P2860
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@en
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@nl
type
label
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@en
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@nl
prefLabel
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@en
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@nl
P2860
P356
P1433
P1476
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560030811
P577
1994-08-01T00:00:00Z