Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes - Wikidata - wikimedia - TriplyDB

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes

http://www.wikidata.org/entity/Q27619558

about

Analyzing effects of naturally occurring missense mutations Interatomic potentials and solvation parameters from protein engineering data for buried residues Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme Effect of foreign N-terminal residues on the conformational stability of human lysozyme Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole Predicting the melting point of human C-type lysozyme mutants Knowledge-based potential defined for a rotamer library to design protein sequences.Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.iStable: off-the-shelf predictor integration for predicting protein stability changes Molecular dynamics study of naturally existing cavity couplings in proteins.Predicting folding free energy changes upon single point mutations Engineering Proteins for Thermostability with iRDP Web Server Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and alpha-lactalbumin.

P2860

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P2860

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes

http://www.wikidata.org/entity/Q27619558

description

1999 nî lūn-bûn

@nan

1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1999年の論文

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1999年論文

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1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

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1999年論文

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1999年论文

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name

Experimental verification of t ...... a using mutant human lysozymes

@ast

Experimental verification of t ...... a using mutant human lysozymes

@en

Experimental verification of t ...... a using mutant human lysozymes

@nl

type

label

Experimental verification of t ...... a using mutant human lysozymes

@ast

Experimental verification of t ...... a using mutant human lysozymes

@en

Experimental verification of t ...... a using mutant human lysozymes

@nl

prefLabel

Experimental verification of t ...... a using mutant human lysozymes

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Experimental verification of t ...... a using mutant human lysozymes

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Experimental verification of t ...... a using mutant human lysozymes

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P1433

Protein Engineering Design and Selection

P1476

Experimental verification of t ...... a using mutant human lysozymes

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P2093

K Nishikawa

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K Ogasahara

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K Takano

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K Yutani

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M Ota

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P2860

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants

Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core

Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences

The structure, stability, and folding process of amyloidogenic mutant human lysozyme

Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants

Contribution of water molecules in the interior of a protein to the conformational stability

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants

A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme

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663-72

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scholarly article

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10.1093/PROTEIN/12.8.663

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8

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12

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10469827

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