Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase (Q43029590)

12 November 2017

title

Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase (English)

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12 November 2017

2

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12 November 2017

Trejo F

1

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12 November 2017

Ferrer A

3

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12 November 2017

Boronat A

4

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12 November 2017

Busquets M

5

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12 November 2017

Cortés A

6

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12 November 2017

publication date

1 November 2001

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Protein Engineering Design and Selection

12 November 2017

published in

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12 November 2017

volume

14

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12 November 2017

issue

11

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12 November 2017

page(s)

911-917

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

12 November 2017

cites work

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https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

The Protein Data Bank: a computer-based archival file for macromolecular structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

A free derivative program for non-linear regression analysis of enzyme kinetics to be used on small computers.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Effects of engineered salt bridges on the stability of subtilisin BPN'

21 January 2018

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https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Designing the hydrophobic core of Thermus flavus malate dehydrogenase based on side-chain packing

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Enhancement of the turnover number of thermostable malate dehydrogenase by deleting hydrogen bonds around the catalytic site.

21 January 2018

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https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase

21 January 2018

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https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

DNA sequencing with chain-terminating inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Heat stability of a tetrameric enzyme, D-glyceraldehyde-3-phosphate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

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

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Relationship of protein flexibility to thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2

21 January 2018

1 reference

https://api.crossref.org/works/10.1093/PROTEIN/14.11.911

10.1093/PROTEIN/14.11.911

21 January 2018

Identifiers

DOI

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12 November 2017

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