Bioinformatics-driven, rational engineering of protein thermostability.

Bioinformatics-driven, rational engineering of protein thermostability. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Bioinformatics-driven, rational engineering of protein thermostability. Abstract Text:

Mary Kate Ditursi,Seok-Joon Kwon,Philippa J Reeder,Jonathan S Dordick,

A longstanding goal in protein engineering is to identify specific sequence changes that endow proteins with desired functional properties. As opposed to traditional rational and random protein engineering techniques, we have employed a bioinformatic approach to identify specific sequence changes that influence key functional properties of a protein within a defined superfamily. Specifically, we have used the Bayesian sequence-based algorithms PROBE and Classifier to identify a strand-turn-strand motif that contributes to thermophilicity among members of the serine protease subtilase superfamily. By replacing a 16 amino acid sequence in the mesophilic subtilisin E (from Bacillus subtilis) with a bioinformatics-generated thermophilic model sequence, the melting temperature of subtilisin E was increased by 13 degrees C. While wild-type subtilisin E was inactive at 90 degrees C, the mutant retained a substantial fraction of its function, with ca. one-third of the activity that it has at 45 degrees C.

Bioinformatics-driven, rational engineering of protein thermostability. Publishing Authors By Initials

MK Ditursi,SJ Kwon,PJ Reeder,JS Dordick,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

PUBMED ID PMID:

MEDLINE DATE:

Bioinformatics-driven, rational engineering of protein thermostability. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Protein engineering, design & selection : PEDS

VOLUME: 19

Page Numbers: 517-24

Journal Abbreviation: Protein Eng. Des. Sel.

ISSN: 1741-0126

DAY: 26

MONTH: 09

YEAR: 2006

Bioinformatics-driven, rational engineering of protein thermostability. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101186484

Bioinformatics-driven, rational engineering of protein thermostability. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: genetics

Chemical & Substance for Abstract: Bioinformatics-driven, rational engineering of protein thermostability. Information

Substance Name: Subtilisins

Registry Number: EC 3.4.21.-

Grant and Affiliation Information for Bioinformatics-driven, rational engineering of protein thermostability.

AFFILIATION: Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute Troy, NY 12180-3590, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM66712

ACRONYM: GM

MEDLINETA: Protein Eng Des Sel

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Bioinformatics-driven, rational engineering of protein thermostability Related Publications

• Active-site titration of serine proteases in organic solvents.
• Bioinformatics-driven, rational engineering of protein thermostability.
• Controlling enzyme-catalyzed regioselectivity in sugar ester synthesis.
• Enzymatic synthesis of a sucrose-containing linear polyester in nearly anhydrous organic media.
• Enzyme activation for organic solvents made easy.
• Enzyme-carbon nanotube conjugates in room-temperature ionic liquids.
• Exploiting the reaction flexibility of a type III polyketide synthase through in vitro pathway manipulation.
• Extraordinary enantiospecificity of lipase catalysis in organic media induced by purification and catalyst engineering.
• Highly active and stable DNAzyme-carbon nanotube hybrids.
• In vitro transcription and protein translation from carbon nanotube-DNA assemblies.
• Lipid-based nanotubes as functional architectures with embedded fluorescence and recognition capabilities.
• Mathematical model for the luminol chemiluminescence reaction catalyzed by peroxidase.
• Mechanism of extraction of chymotrypsin into isooctane at very low concentrations of aerosol OT in the absence of reversed micelles.
• Numerical and Monte Carlo simulations of phenolic polymerizations catalyzed by peroxidase.
• On-chip, cell-based microarray immunofluorescence assay for high-throughput analysis of target proteins.
• Organic solvents strip water off enzymes.
• Polymer-nanotube-enzyme composites as active antifouling films.
• Pressure affects enzyme function in organic media.
• Rheumatoid arthritis in the elderly.
• Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes.
• The effect of high temperature and humidity upon cattle.
• The role of the methoxyphenol apocynin, a vascular NADPH oxidase inhibitor, as a chemopreventative agent in the potential treatment of cardiovascular diseases.
• Three-dimensional cellular microarray for high-throughput toxicology assays.
• Unusual salt and solvent dependence of a protease from an extreme halophile.