The effect of net charge on the solubility, activity, and stability of ribonuclease Sa - Wikidata - wikimedia - TriplyDB

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

http://www.wikidata.org/entity/Q28365668

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Macromolecule-assisted de novo protein folding X-ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity The contribution of polar group burial to protein stability is strongly context-dependent Solution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeonThermococcus celer Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins Cytotoxic ribonucleases: molecular weapons and their targets Protein Thermostability Is Owing to Their Preferences to Non-Polar Smaller Volume Amino Acids, Variations in Residual Physico-Chemical Properties and More Salt-Bridges Empirical relationships between protein structure and carboxyl pKa values in proteins.Protein structure, stability and solubility in water and other solvents.Microbial ribonucleases (RNases): production and application potential.Thermodynamic parameters for salt-induced reversible protein precipitation from automated microscale experiments.High-throughput thermal stability analysis of a monoclonal antibody by attenuated total reflection FT-IR spectroscopic imaging.Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein Site-specific contributions to the pH dependence of protein stability Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.SCHEMA-designed variants of human Arginase I and II reveal sequence elements important to stability and catalysis.Mechanisms of protein sequence divergence and incompatibility.On-line capillary isoelectric focusing hyphenated to native electrospray ionization mass spectrometry for the characterization of interferon-γ and variants.Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation Carboxyl pK(a) values, ion pairs, hydrogen bonding, and the pH-dependence of folding the hyperthermophile proteins Sac7d and Sso7d Increasing protein conformational stability by optimizing beta-turn sequence Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.Salt-induced stabilization of apoflavodoxin at neutral pH is mediated through cation-specific effects.Prediction of protein solubility from calculation of transfer free energy.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.Revisiting ligand-induced conformational changes in proteins: essence, advancements, implications and future challenges.Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic.Binase cleaves cellular noncoding RNAs and affects coding mRNAs.Increasing protein stability: importance of DeltaC(p) and the denatured state.Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp.Unveiling the optimal parameters for cellulolytic characteristics of Talaromyces verruculosus SGMNPf3 and its secretory enzymes.Cytotoxicity of RNase Sa to the acute myeloid leukemia Kasumi-1 cells depends on the net charge.Calibrative approaches to protein solubility modeling of a mutant series using physicochemical descriptors.Limitation of tuning the antibody-antigen reaction by changing the value of pH and its consequence for hyperthermia A summary of the measured pK values of the ionizable groups in folded proteins.The role of protein stability, solubility, and net charge in amyloid fibril formation.Practical insights on enzyme stabilization.pK values of the ionizable groups of proteins.Polyarginine as a multifunctional fusion tag.

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P2860

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

http://www.wikidata.org/entity/Q28365668

description

2001 nî lūn-bûn

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2001 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2001 թվականի հունիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年论文

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name

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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type

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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prefLabel

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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Protein Science

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The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

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A A Makarov

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C N Pace

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G I Yakovlev

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G R Grimsley

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K L Shaw

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P2860

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Contribution of salt bridges near the surface of a protein to the conformational stability

Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis

Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability

Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1

The interpretation of protein structures: estimation of static accessibility

Electrostatic contributions to molecular free energies in solution

Electrophoresis buffers for polyacrylamide gels at various pH

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme

pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds

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10.1110/PS.440101

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11369859

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