Protein rigidity and thermophilic adaptation (Q43030167)

12 November 2017

Protein rigidity and thermophilic adaptation (English)

1 reference

12 November 2017

Sebastian Radestock

1

1 reference

PubMed ID

21246632

12 November 2017

Holger Gohlke

series ordinal

2

1 reference

PubMed ID

21246632

12 November 2017

language of work or name

English

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publication date

18 January 2011

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12 November 2017

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12 November 2017

79

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12 November 2017

4

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12 November 2017

1089-1108

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The stability of proteins in extreme environments

12 November 2017

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Thermophilic adaptation of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Review: Protein function at thermal extremes: balancing stability and flexibility

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Enzymes from extremophiles

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Recent progress towards the application of hyperthermophiles and their enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Potential and utilization of thermophiles and thermostable enzymes in biorefining

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

High-throughput screening for enhanced protein stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Rational engineering of enzyme stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Directed evolution of enzyme stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Engineering thermostability: lessons from thermophilic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Better library design: data-driven protein engineering

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Lessons in stability from thermophilic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Physics and evolution of thermophilic adaptation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein and DNA sequence determinants of thermophilic adaptation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Effective factors in thermostability of thermophilic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Factors enhancing protein thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein thermal stability: hydrogen bonds or internal packing?

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein stability and molecular adaptation to extreme conditions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The complex inter-relationships between protein flexibility and stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Some like it cold: biocatalysis at low temperatures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Molecular dynamics studies on the thermostability of family 11 xylanases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: thermal stability of protein domains and unfolding pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein unfolding behavior studied by elastic network model

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Multiscale modeling of macromolecular conformational changes combining concepts from rigidity and elastic network theory.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

A natural coarse graining for simulating large biomolecular motion

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein flexibility predictions using graph theory

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Dominant forces in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Network analysis of protein dynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Uncovering network systems within protein structures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Protein unfolding: rigidity lost

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Automated design of the surface positions of protein helices

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Statistical mechanics of complex networks

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Cluster size diversity, percolation, and complex systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Change in protein flexibility upon complex formation: analysis of Ras-Raf using molecular dynamics and a molecular framework approach.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

High thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus resulting from low DeltaC(p) of unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Urea-induced unfolding and conformational stability of 3-isopropylmalate dehydrogenase from the Thermophile thermus thermophilus and its mesophilic counterpart from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Increased thermal stability against irreversible inactivation of 3-isopropylmalate dehydrogenase induced by decreased van der Waals volume at the subunit interface

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Stabilization of Escherichia coli isopropylmalate dehydrogenase by single amino acid substitution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Mirror image mutations reveal the significance of an intersubunit ion cluster in the stability of 3-isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus, by constructing chimeric enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Effect of polar side chains at position 172 on thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Screening of stable proteins in an extreme thermophile, Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

A new way of enhancing the thermostability of proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Engineering an enzyme to resist boiling

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Analysis of structural determinants of the stability of thermolysin-like proteases by molecular modelling and site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Introduction of a stabilizing 10 residue beta-hairpin in Bacillus subtilis neutral protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Cumulative stabilizing effects of glycine to alanine substitutions in Bacillus subtilis neutral protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Modeling virus self-assembly pathways: avoiding dynamics using geometric constraint decomposition

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Conserved quantitative stability/flexibility relationships (QSFR) in an orthologous RNase H pair

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein family

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structural distribution of stability in a thermophilic enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Reduced temperature dependence of collective conformational opening in a hyperthermophile rubredoxin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Cold adaptation of the thermophilic enzyme 3-isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Analysis of the effect of accumulation of amino acid replacements on activity of 3-isopropylmalate dehydrogenase from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Probing catalytic hinge bending motions in thermolysin-like proteases by glycine --> alanine mutations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structural analysis of zinc substitutions in the active site of thermolysin

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Conformational dynamics of free and catalytically active thermolysin are indistinguishable by hydrogen/deuterium exchange mass spectrometry

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Improving the activity and stability of thermolysin by site-directed mutagenesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Small-world view of the amino acids that play a key role in protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Topological determinants of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Side-chain clusters in protein structures and their role in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Identification of side-chain clusters in protein structures by a graph spectral method.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

A network representation of protein structures: implications for protein stability.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Computational thermostabilization of an enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Native protein sequences are close to optimal for their structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Design, structure and stability of a hyperthermophilic protein variant

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The distribution and query systems of the RCSB Protein Data Bank

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Errors in protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

DaliLite workbench for protein structure comparison

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

ProTherm, version 4.0: thermodynamic database for proteins and mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Revisiting the correlation between proteins' thermoresistance and organisms' thermophilicity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

Relationship of protein flexibility to thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

The essential dynamics of thermolysin: Confirmation of the hinge-bending motion and comparison of simulations in vacuum and water

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FPROT.22946

21 January 2018

Identifiers

DOI

10.1002/PROT.22946

1 reference

12 November 2017

1 reference

PubMed ID

21246632