Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C.
about
Near-atomic resolution neutron crystallography on perdeuterated Pyrococcus furiosus rubredoxin: implication of hydronium ions and protonation state equilibria in redox changesHyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostabilityHigh stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactorsMechanism of pressure-induced thermostabilization of proteins: studies of glutamate dehydrogenases from the hyperthermophile Thermococcus litoralisBetter biomolecule thermodynamics from kinetics.The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.pH dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.The thermophilic esterase from Archaeoglobus fulgidus: structure and conformational dynamics at high temperature.Thermal stability of Clostridium pasteurianum rubredoxin: deconvoluting the contributions of the metal site and the protein.Femtosecond dynamics of rubredoxin: tryptophan solvation and resonance energy transfer in the protein.Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.Cytochrome c folding pathway: kinetic native-state hydrogen exchange.Cooperative folding units of escherichia coli tryptophan repressor.An amino acid code for protein foldingMillisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature.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 structureDo ultrastable proteins from hyperthermophiles have high or low conformational rigidity?Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoesLessons in stability from thermophilic proteins.Some thermodynamic implications for the thermostability of proteins.Structural distribution of stability in a thermophilic enzymePreliminary neutron crystallographic analysis of selectively CH3-protonated deuterated rubredoxin from Pyrococcus furiosusThermodynamic stability and folding of proteins from hyperthermophilic organisms.Neutron crystallographic study on rubredoxin from Pyrococcus furiosus by BIX-3, a single-crystal diffractometer for biomacromolecules.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersSpatial distribution of dielectric shielding in the interior of Pyrococcus furiosus rubredoxin as sampled in the subnanosecond timeframe by hydrogen exchange.Surface salt bridges stabilize the GCN4 leucine zipper.Chaperonin function: folding by forced unfolding.Determinants of protein hydrogen exchange studied in equine cytochrome c.Factors enhancing protein thermostability.Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases.The esterase from the thermophilic eubacterium Bacillus acidocaldarius: structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus.High thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus resulting from low DeltaC(p) of unfolding.Protein hydrogen exchange mechanism: local fluctuations.Additivity of differential conformational dynamics in hyperthermophile/mesophile rubredoxin chimeras as monitored by hydrogen exchange.
P2860
Q27683576-D9C56756-71A2-48BE-B135-D3E33F83AC62Q28203641-D227EF60-427F-4D76-A7D5-2AFFBBEDEA63Q28344759-4FBA0C92-80C1-4A77-9A45-DD5E457CAEA3Q28346474-A47B8637-2721-4E20-B410-6F4814489061Q30010275-B72E2DA0-339B-485B-8981-DAF7C8EB1606Q30165217-19EB0509-714B-42E3-9283-5BEC416C7896Q30165497-E0CDD5F9-5B11-4C9C-A2B4-C4193A9FCBC8Q30326370-AA497D26-8E17-40E0-BAAF-4058C6BF420DQ30327883-F0FF7354-25FB-4023-8CE0-41F092A65B89Q30329283-20F13358-4A1F-40BA-8842-F96DEAAA5B03Q30873433-CFA273A6-567A-4CAA-91F9-BC7747B5ADB7Q34155517-7AAC1237-D175-4765-8AB8-3020DDFB9763Q34171368-BB07C9D9-199C-44D2-9ED2-2F2FF456A461Q34584803-010D0BAB-CD8C-4DF0-89BB-1CEA11C8990EQ35107288-D441F59A-C7FD-4A25-8FF9-ED50D6950A9CQ35113355-08F35397-8376-4246-ADFD-D4D9D1B511E0Q36198595-3EBE21B1-0C23-46D5-8FBC-3CB2E77C00E4Q36367292-CDBCCFD0-CCC3-4396-AD32-0EFDDC88F936Q36525476-215A76A9-08D3-4E4C-A262-E0B705998B26Q36640421-1424F138-4B4B-4DBA-861E-D9DAF456CD2FQ36698879-1970CD41-477D-4574-A49D-3BB86AA0A25EQ36812468-CF6F5084-A81D-42FE-AE9E-6ADDBDCB8AFCQ36903897-52839C9F-5A1D-4969-8F22-65B94E2D9DFDQ37388518-772C064B-0D10-4AD1-A232-AF160A6D44BCQ37727718-C40116CD-0764-4E5B-A0CC-754493348309Q39717727-859164EA-ED80-4523-954B-8A1B2166A7FEQ42090008-B2F263D9-356B-432F-BB60-65BF16FF6501Q42097312-D4B8C049-8173-4CDE-BE3F-D7F29B17FF1DQ42846376-2EAE22E8-199A-44D9-8B5D-0CF0053F124AQ43027455-D2D64B2E-CFBB-4C08-85A7-D08453CCD866Q43027594-B16AF875-5BBA-4D45-B3F6-9FD35754FF1CQ43027699-6D129FEA-FB38-496F-9596-C012853DA653Q43029793-0B415FB0-7FBC-481F-BEF4-AD81636A5F39Q43137301-0195D135-DAAE-4B9F-B028-0B854C4D9915Q51930102-5FAAA6E1-41FF-4832-854F-BA1A3D89B0AF
P2860
Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@ast
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@en
type
label
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@ast
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@en
prefLabel
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@ast
Stability and dynamics in a hy ...... rature close to 200 degrees C.
@en
P2093
P2860
P356
P1476
Stability and dynamics in a hy ...... erature close to 200 degrees C
@en
P2093
P2860
P304
11329-11332
P356
10.1073/PNAS.94.21.11329
P407
P577
1997-10-01T00:00:00Z