Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart. - Wikidata - awgldk - TriplyDB

Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart.

Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart.

http://www.wikidata.org/entity/Q43698043

about

Laboratory evolution of Pyrococcus furiosus alcohol dehydrogenase to improve the production of (2S,5S)-hexanediol at moderate temperatures.Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding.Catalyzing "hot" reactions: enzymes from hyperthermophilic Archaea.Stability curve prediction of homologous proteins using temperature-dependent statistical potentials Role of residual structure in the unfolded state of a thermophilic protein.Lessons in stability from thermophilic proteins.Thermodynamic stability and folding of proteins from hyperthermophilic organisms.Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.Biochemical Characterization, Thermal Stability, and Partial Sequence of a Novel Exo-Polygalacturonase from the Thermophilic Fungus Rhizomucor pusillus A13.36 Obtained by Submerged Cultivation.Molecular bases of thermophily in hyperthermophiles.Genome stability: recent insights in the topoisomerase reverse gyrase and thermophilic DNA alkyltransferase.How do thermophilic proteins and proteomes withstand high temperature?Alkylation damage repair protein O6-alkylguanine-DNA alkyltransferase from the hyperthermophiles Aquifex aeolicus and Archaeoglobus fulgidus.Protein thermostabilizing factors: high relative occurrence of amino acids, residual properties, and secondary structure type in different residual state.The stability of Taq DNA polymerase results from a reduced entropic folding penalty; identification of other thermophilic proteins with similar folding thermodynamics.

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Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart.

http://www.wikidata.org/entity/Q43698043

description

2001 nî lūn-bûn

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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name

Comparative analyses of the co ...... nd its mesophilic counterpart.

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Comparative analyses of the co ...... nd its mesophilic counterpart.

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type

label

Comparative analyses of the co ...... nd its mesophilic counterpart.

@en

Comparative analyses of the co ...... nd its mesophilic counterpart.

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prefLabel

Comparative analyses of the co ...... nd its mesophilic counterpart.

@en

Comparative analyses of the co ...... nd its mesophilic counterpart.

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Comparative analyses of the co ...... nd its mesophilic counterpart.

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K Shiraki

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P2860

Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase

Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

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

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability

Calculation of protein extinction coefficients from amino acid sequence data

Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions.

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