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Rigidity of Thermophilic Enzymes
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scholarly article
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title
Rigidity of Thermophilic Enzymes
(English)
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author name string
Angelo Fontana
series ordinal
1
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Vincenzo De Filippis
series ordinal
2
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Patrizia Polverino de Laureto
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3
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Elena Scaramella
series ordinal
4
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Marcello Zambonin
series ordinal
5
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publication date
1998
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published in
Progress in biotechnology
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page(s)
277-294
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cites work
Enzymes and proteins from organisms that grow near and above 100 degrees C.
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Extremozymes: expanding the limits of biocatalysis
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Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
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Mutational effects on protein stability
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Thermal stability and protein structure
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Enzyme engineering reaches the boiling point
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Improvement of thermal stability of subtilisin J by changing the primary autolysis site
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Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme
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Enolase from the thermophile Thermus X-1
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Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase
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Incorporation of a stabilizing Ca(2+)-binding loop into subtilisin BPN'
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Large differences in the helix propensities of alanine and glycine.
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Enzyme thermostability and thermoactivity
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Enhanced protein thermostability by Ala-->Aib replacement
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Correlation of hydrogen exchange behaviour and thermal stability of lysozyme
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Dominant forces in protein folding
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Exposure of tryptophanyl residues and protein dynamics
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Fluorescence quenching studies with proteins
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Understanding and increasing protein stability
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Psychrophilic enzymes: molecular basis of cold adaptation
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Analysis and modulation of protein stability
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Correlation between sites of limited proteolysis and segmental mobility in thermolysin
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Purification and Properties of d-Glyceraldehyde-3-Phosphate Dehydrogenase from an Extreme Thermophile, Thermus thermophilus Strain HB 8
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Psychrophilic enzymes: a thermodynamic challenge
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Intracellular protein degradation in mammalian and bacterial cells
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Isocitrate Lyase from a Thermophilic Bacillus : Effect of Salts on Enzyme Activity
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Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents
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Motions in Proteins
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Esterase activity of zinc neutral proteases
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Enzymes under extremes of physical conditions
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Protein stability and molecular adaptation to extreme conditions
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Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles.
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Remarkable activity enhancement of thermolysin mutants
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How do enzymes work?
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Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin
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Cumulative stabilizing effects of glycine to alanine substitutions in Bacillus subtilis neutral protease
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Substantial increase of protein stability by multiple disulphide bonds
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Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein
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Genetic and structural analysis of the protein stability problem
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Structural and genetic analysis of protein stability
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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
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Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices.
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Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix
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Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
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Predicting Ca(2+)-binding sites in proteins
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Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase alpha subunit
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A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
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Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
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Analysis of protein conformational characteristics related to thermostability
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Hyperthermophiles: taking the heat and loving it.
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The Structural and Functional Roles of Metal Ions in Thermolysin
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Engineering thermostability: lessons from thermophilic proteins
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A relationship between protein stability and protein function
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Structural features of neutral protease from Bacillus subtilis deduced from model-building and limited proteolysis experiments.
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Proteins and temperature
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A thermostable enolase from the extreme thermophile Thermus aquaticus YT-1.
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Malate dehydrogenase from thermophilic and mesophilic bacteria. Molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity
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Abnormally high tolerance against proteolysis of an exo-oligo-1,6-glucosidase from a thermophile Bacillus thermoglucosidius KP 1006, compared with its mesophilic counterpart from Bacillus cereus ATCC 7064
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Protein metal-binding sites
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Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease
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Rendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission.
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Engineering an enzyme to resist boiling
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Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
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Thermozymes.
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Relationship of protein flexibility to thermostability
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Accuracy of protein flexibility predictions
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Protein thermal stability, hydrogen bonds, and ion pairs
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Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
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Additivity of mutational effects in proteins
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Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
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Glycine residues provide flexibility for enzyme active sites
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Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
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10.1016/S0921-0423(98)80043-9
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