(Q27619558)

1

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M Ota

2

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K Ogasahara

3

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Y Yamagata

4

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K Nishikawa

5

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K Yutani

Protein Engineering Design and Selection

6

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publication date

August 1999

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published in

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volume

12

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issue

8

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page(s)

663-72

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cites work

High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation.

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A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

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

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Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with x-ray structure analysis of proline mutants

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

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Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants

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Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond

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

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Hydrogen bonding stabilizes globular proteins

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Desk-top analysis of the structural stability of various point mutations introduced into ribonuclease H.

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Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface.

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Isolation and characterization of human milk lysozyme.

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Empirical scale of side-chain conformational entropy in protein folding

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Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

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A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study

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A 3D-1D substitution matrix for protein fold recognition that includes predicted secondary structure of the sequence

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Hydrophobic basis of packing in globular proteins

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An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction

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Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.

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

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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

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

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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

21 January 2018

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

21 January 2018

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Statistical potentials extracted from protein structures: how accurate are they?

21 January 2018

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Prediction of the stability of protein mutants based on structural environment-dependent amino acid substitution and propensity tables

21 January 2018

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

21 January 2018

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Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit

21 January 2018

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Novel knowledge-based mean force potential at atomic level

21 January 2018

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In search of European excellence

21 January 2018

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Context-dependent secondary structure formation of a designed protein sequence

21 January 2018

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