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Increasing protein stability by altering long-range coulombic interactions.

Increasing protein stability by altering long-range coulombic interactions.

http://www.wikidata.org/entity/Q36281644

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Mutation of exposed hydrophobic amino acids to arginine to increase protein stability Solution structure and dynamics of ribonuclease Sa The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges 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 Crystal Structure of D-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability An Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants from Alicyclobacillus acidocaldarius Rational stabilization of enzymes by computational redesign of surface charge-charge interactions The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity Electrostatic Contribution of Surface Charge Residues to the Stability of a Thermophilic Protein: Benchmarking Experimental and Predicted pKa Values Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability Structure of a thermophilic cyanobacterial b6f-type Rieske protein The effect of net charge on the solubility, activity, and stability of ribonuclease Sa Positive selection in octopus haemocyanin indicates functional links to temperature adaptation Free energy determinants of tertiary structure and the evaluation of protein models.Protein structure, stability and solubility in water and other solvents.Electrostatic contributions to the kinetics and thermodynamics of protein assembly Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles.The effects of NaCl concentration and pH on the stability of hyperthermophilic protein Ssh10b.Engineering thermal stability of L-asparaginase by in vitro directed evolution.Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability The role of surface electrostatics on the stability, function and regulation of human cystathionine β-synthase, a complex multidomain and oligomeric protein Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.Relationship between ion pair geometries and electrostatic strengths in proteins.Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin 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 Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge charge interactions Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments.Salt-induced stabilization of apoflavodoxin at neutral pH is mediated through cation-specific effects.Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction Some like it hot: the molecular determinants of protein thermostability.The ruggedness of protein-protein energy landscape and the cutoff for 1/r(n) potentials.

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P2860

Increasing protein stability by altering long-range coulombic interactions.

http://www.wikidata.org/entity/Q36281644

description

1999 nî lūn-bûn

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1999年の論文

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1999年学术文章

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1999年学术文章

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1999年学术文章

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1999年学术文章

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1999年学术文章

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1999年學術文章

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1999年學術文章

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1999年學術文章

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name

Increasing protein stability by altering long-range coulombic interactions.

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Increasing protein stability by altering long-range coulombic interactions.

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type

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Increasing protein stability by altering long-range coulombic interactions.

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Increasing protein stability by altering long-range coulombic interactions.

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Increasing protein stability by altering long-range coulombic interactions.

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Increasing protein stability by altering long-range coulombic interactions.

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Protein Science

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Increasing protein stability by altering long-range coulombic interactions.

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P2093

B M Huyghues-Despointes

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C N Pace

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G R Grimsley

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J M Scholtz

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K L Shaw

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L R Fee

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R L Thurlkill

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R W Alston

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P2860

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

Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive

Design, structure and stability of a hyperthermophilic protein variant

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

Coulombic effects of remote subsites on the active site of ribonuclease A

How to measure and predict the molar absorption coefficient of a protein

The interpretation of protein structures: estimation of static accessibility

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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1843-1849

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10.1110/PS.8.9.1843

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9

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10493585

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2144408

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