Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. - Wikidata - wikimedia - TriplyDB

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

http://www.wikidata.org/entity/Q43030179

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Optimization to low temperature activity in psychrophilic enzymes Functional motions of Candida antarctica lipase B: a survey through open-close conformations Crystal structure of a cold-adapted class C beta-lactamase Destabilization of psychrotrophic RNase HI in a localized fashion as revealed by mutational and X-ray crystallographic analyses Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes A comparative study of cold- and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulations Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutations PROMPT: a protein mapping and comparison tool Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins Mechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii.The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility Natural selection of more designable folds: a mechanism for thermophilic adaptation.Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Mutational analysis of the Escherichia coli DEAD box protein CsdA Coping with our cold planet Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1.Kinetic and thermodynamic studies of peptidyltransferase in ribosomes from the extreme thermophile Thermus thermophilus.Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility an Psychrophilic enzymes: from folding to function and biotechnology.Amino acid cost and codon-usage biases in 6 prokaryotic genomes: a whole-genome analysis.Extremophilic SHMTs: from structure to biotechnology.A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering.Determinants of Thermostability in Serine Hydroxymethyltransferase Identified by Principal Component Analysis.Sequence-based analysis of protein energy landscapes reveals nonuniform thermal adaptation within the proteome.Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis Adaptation of class-13 alpha-amylases to diverse living conditions.Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases.Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.Structural adaptation to low temperatures--analysis of the subunit interface of oligomeric psychrophilic enzymes.Protein rigidity and thermophilic adaptation.Activity-stability relationships in extremophilic enzymes.Protein flexibility in psychrophilic and mesophilic trypsins. Evidence of evolutionary conservation of protein dynamics in trypsin-like serine-proteases.Purification, characterization, and overexpression of psychrophilic and thermolabile malate dehydrogenase of a novel antarctic psychrotolerant, Flavobacterium frigidimaris KUC-1.Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes.Exploring the influence of hyperthermophilic protein Ssh10b on the stability and conformation of RNA by molecular dynamics simulation.Homologous yeast lipases/acyltransferases exhibit remarkable cold-active properties

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P2860

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

http://www.wikidata.org/entity/Q43030179

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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name

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@en

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@nl

type

label

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@en

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@nl

prefLabel

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@en

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@nl

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Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

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Francesco Bossa

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Giulio Gianese

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Stefano Pascarella

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P2860

Improved tools for biological sequence comparison.

PROCHECK: a program to check the stereochemical quality of protein structures

Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum

Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme

Structure of lobster apo-D-glyceraldehyde-3-phosphate dehydrogenase at 3.0 A resolution

Cold adaption of enzymes: structural comparison between salmon and bovine trypsins

Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 A resolution

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

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

Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 A resolution

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236-249

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scholarly article

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10.1002/PROT.10084

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2

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