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Hyperthermophile protein behavior: partially-structured conformations of Pyrococcus furiosus rubredoxin monomers generated through forced cold-denaturation and refoldingFolding of beta/alpha-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (beta/alpha)8-barrel.Manipulation of unfolding-induced protein aggregation by peptides selected for aggregate-binding ability through phage display library screening.Confocal spectrofluorimetric evidence for the hetero-aggregation of sequence-scrambled forms of two model all-beta sheet proteins.Identification and characterization of a spontaneously aggregating amyloid-forming variant of human PrP((90-231)) through phage-display screening of variants randomized between residues 101 and 112.Folding behavior of a backbone-reversed protein: reversible polyproline type II to beta-sheet thermal transitions in retro-GroES multimers with GroES-like features.Solution-state characteristics of the ultraviolet A-induced visible fluorescence from proteins.N-Terminal sequencing by mass spectrometry through specific fluorescamine labeling of α-amino groups before tryptic digestion.The key to the extraordinary thermal stability of P. furiosus holo-rubredoxin: iron binding-guided packing of a core aromatic cluster responsible for high kinetic stability of the native structureCalcium binding to beta-2-microglobulin at physiological pH drives the occurrence of conformational changes which cause the protein to precipitate into amorphous forms that subsequently transform into amyloid aggregates.Direct N-terminal sequencing of polypeptides using a thermostable bacterial aminopeptidase and MALDI-TOF mass spectrometry.Metal-catalyzed proteolysis, conformational antigenicity, photosensitized oxidation, and electrical dysfunction explain the pathogenicity of protein aggregates.Probing protease sensitivity of recombinant human erythropoietin reveals α3-α4 inter-helical loop as a stability determinant.Protein engineering of domains in flavoprotein disulphide oxidoreductases: contributions to folding and assembly.'Super-perfect' enzymes: Structural stabilities and activities of recombinant triose phosphate isomerases from Pyrococcus furiosus and Thermococcus onnurineus produced in Escherichia coli.Endoglucanase activity at a second site in Pyrococcus furiosus triosephosphate isomerase-Promiscuity or compensation for a metabolic handicap?Use of a hydrophobic dye to indirectly probe the structural organization and conformational plasticity of molecules in amorphous aggregates of carbonic anhydrase.Design of a soluble mini-protein through tandem duplication of the minimally engineered beta hairpin 'tongue' motif of alpha-hemolysin.A backbone-reversed form of an all-beta alpha-crystallin domain from a small heat-shock protein (retro-HSP12.6) folds and assembles into structured multimers.Expression, purification, refolding and characterization of a putative lysophospholipase from Pyrococcus furiosus: retention of structure and lipase/esterase activity in the presence of water-miscible organic solvents at high temperatures.The excised heat-shock domain of alphaB crystallin is a folded, proteolytically susceptible trimer with significant surface hydrophobicity and a tendency to self-aggregate upon heating.Direct proteolysis-based purification of an overexpressed hyperthermophile protein from Escherichia coli lysate: a novel exploitation of the link between structural stability and proteolytic resistance.Creation of active TIM barrel enzymes through genetic fusion of half-barrel domain constructs derived from two distantly related glycosyl hydrolases.Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA).Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein.Slow irreversible unfolding of Pyrococcus furiosus triosephosphate isomerase: separation and quantitation of conformers through a novel electrophoretic approach.Characterization of a mildly alkalophilic and thermostable recombinant Thermus thermophilus laccase with applications in decolourization of dyes.Probing the excited state dynamics of Venus: origin of dual-emission in fluorescent proteins.Single cell-level detection and quantitation of leaky protein expression from any strongly regulated bacterial system.Structures of differently aggregated and precipitated forms of gamma B crystallin: an FTIR spectroscopic and EM study.Arsenic and 17-β-estradiol bind to each other and neutralize each other's signaling effects.The Achilles' Heel of "Ultrastable" Hyperthermophile Proteins: Submillimolar Concentrations of SDS Stimulate Rapid Conformational Change, Aggregation, and Amyloid Formation in Proteins Carrying Overall Positive Charge.Attenuation of ionic interactions profoundly lowers the kinetic thermal stability of Pyrococcus furiosus triosephosphate isomerase.Coalescence of spherical beads of retro-HSP12.6 into linear and ring-shaped amyloid nanofibers.Cooperative relaxation of supercoils and periodic transcriptional initiation within polymerase batteries.Hydroxyl radical mediated damage to proteins, with special reference to the crystallinsUse of tandem cuvettes to determine whether radiative (trivial) energy transfer can contaminate steady-state measurements of fluorescence resonance energy transferHydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refoldingPeptide scanning-based identification of regions of gamma-II crystallin involved in thermal aggregation: evidence of the involvement of structurally analogous, helix-containing loops from the two double Greek key domains of the moleculeEvidence of native-like substructure(s) in polypeptide chains of carbonic anhydrase deposited into insoluble aggregates during thermal unfolding
P50
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Forscher
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P Guptasarma
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P31
P496
0000-0002-4801-3180