Optimization of the electrostatic interactions in proteins of different functional and folding type.
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Engineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structureRemoval of surface charge-charge interactions from ubiquitin leaves the protein folded and very stableFree energy determinants of tertiary structure and the evaluation of protein models.The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions.Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima.Theoretical and experimental study of the D2194G mutation in the C2 domain of coagulation factor V.Cation selective promotion of tubulin polymerization by alkali metal chloridesBackbone makes a significant contribution to the electrostatics of alpha/beta-barrel proteins.Increasing protein stability by altering long-range coulombic interactions.Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments.Some like it hot: the molecular determinants of protein thermostability.Rapid comparison of properties on protein surfaceProtein ionizable groups: pK values and their contribution to protein stability and solubility.Forces stabilizing proteinsThermostabilization of proteins by diglycerol phosphate, a new compatible solute from the hyperthermophile Archaeoglobus fulgidus.Optimization of electrostatic interactions in protein-protein complexes.Electrostatic coupling to pH-titrating sites as a source of cooperativity in protein-ligand binding.The dominant role of side-chain backbone interactions in structural realization of amino acid code. ChiRotor: a side-chain prediction algorithm based on side-chain backbone interactionsCharge-charge interactions influence the denatured state ensemble and contribute to protein stability.Optimization of the electrostatic interactions between ionized groups and peptide dipoles in proteins.Molecular dynamics simulations of the thermal stability of tteRBP and ecRBP.Side chain dynamics and alternative hydrogen bonding in the mechanism of protein thermostabilization.Thermophilicity of wild type and mutant cold shock proteins by molecular dynamics simulation.
P2860
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P2860
Optimization of the electrostatic interactions in proteins of different functional and folding type.
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
Optimization of the electrosta ...... t functional and folding type.
@en
type
label
Optimization of the electrosta ...... t functional and folding type.
@en
prefLabel
Optimization of the electrosta ...... t functional and folding type.
@en
P2093
P2860
P356
P1433
P1476
Optimization of the electrosta ...... t functional and folding type.
@en
P2093
Karshikoff AD
Ladenstein R
Spassov VZ
P2860
P304
P356
10.1002/PRO.5560030921
P577
1994-09-01T00:00:00Z