Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability
about
The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different FactorsThe effect of net charge on the solubility, activity, and stability of ribonuclease SaRemoval of surface charge-charge interactions from ubiquitin leaves the protein folded and very stablePrinciples of protein folding--a perspective from simple exact models.Contribution of protein charge to partitioning in aqueous two-phase systems.Distance dependence and salt sensitivity of pairwise, coulombic interactions in a proteinA Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteinsSalt effects on ionization equilibria of histidines in myoglobinElectrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.Evolutionary biochemistry: revealing the historical and physical causes of protein properties.Mutational studies of protein structures and their stabilities.Control of electrostatic interactions between F-actin and genetically modified lysozyme in aqueous media.Crystal structure of activated tobacco rubisco complexed with the reaction-intermediate analogue 2-carboxy-arabinitol 1,5-bisphosphate.Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations.Delineation of an evolutionary salvage pathway by compensatory mutations of a defective lysozyme.Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments.Rapid in vitro screening for the location-dependent effects of unnatural amino acids on protein expression and activity.Exploring the functional robustness of an enzyme by in vitro evolutionDevelopment of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability.Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.The magnitude of changes in guanidine-HCl unfolding m-values in the protein, iso-1-cytochrome c, depends upon the substructure containing the mutationSide chain dynamics and alternative hydrogen bonding in the mechanism of protein thermostabilization.Amino-Acid Network Clique Analysis of Protein Mutation Non-Additive Effects: A Case Study of Lysozme.
P2860
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P2860
Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability
description
1991 nî lūn-bûn
@nan
1991 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Cumulative site-directed charg ...... te little to protein stability
@ast
Cumulative site-directed charg ...... te little to protein stability
@en
Cumulative site-directed charg ...... te little to protein stability
@nl
type
label
Cumulative site-directed charg ...... te little to protein stability
@ast
Cumulative site-directed charg ...... te little to protein stability
@en
Cumulative site-directed charg ...... te little to protein stability
@nl
prefLabel
Cumulative site-directed charg ...... te little to protein stability
@ast
Cumulative site-directed charg ...... te little to protein stability
@en
Cumulative site-directed charg ...... te little to protein stability
@nl
P2093
P1476
Cumulative site-directed charg ...... te little to protein stability
@en
P2093
B W Matthews
E Söderlind
J A Wozniak
P304
P356
10.1016/0022-2836(91)80181-S
P407
P577
1991-10-05T00:00:00Z