The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins.
about
Protein thermal stability enhancement by designing salt bridges: a combined computational and experimental studyEntropic stabilization of proteins and its proteomic consequencesSolution structure of the RNA polymerase subunit RPB5 from Methanobacterium thermoautotrophicumThe crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenaxStructural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridgingPreliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilusStepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophileSolution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeonThermococcus celerAn Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants from Alicyclobacillus acidocaldariusCrystal structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon in a dimeric formUPF201 Archaeal Specific Family Members Reveal Structural Similarity to RNA-Binding Proteins but Low Likelihood for RNA-Binding FunctionCrystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus--structural basis of substrate recognitionStructure, Function, and Targets of the Transcriptional Regulator SvtR from the Hyperthermophilic Archaeal Virus SIRV1Stabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of UnfoldingSerial Femtosecond Crystallography of G Protein-Coupled ReceptorseIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joiningMultiple Conformations of the Loop Region Confers Heat-Resistance on SsArd1, a Thermophilic NatAHyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostabilityThe effect of net charge on the solubility, activity, and stability of ribonuclease SaCorrelated electrostatic mutations provide a reservoir of stability in HIV proteaseConstruction of a cellulase hyper-expression system in Trichoderma reesei by promoter and enzyme engineeringElectrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers.Protein structure, stability and solubility in water and other solvents.Contribution of salt bridges toward protein thermostability.Highly expressed and slowly evolving proteins share compositional properties with thermophilic proteinsMolecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsThermal stability and aggregation of sulfolobus solfataricus beta-glycosidase are dependent upon the N-epsilon-methylation of specific lysyl residues: critical role of in vivo post-translational modifications.Environment specific substitution tables for thermophilic proteins"Hot cores" in proteins: comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms.Discrimination of thermophilic and mesophilic proteins.Evaluating the strength of salt bridges: a comparison of current biomolecular force fields.Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaeaEnhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways.Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditionsElectrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.Relationship between ion pair geometries and electrostatic strengths in proteins.Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding.Modeling the binding sites of anti-hen egg white lysozyme antibodies HyHEL-8 and HyHEL-26: an insight into the molecular basis of antibody cross-reactivity and specificityMillisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature.Protein thermostability prediction within homologous families using temperature-dependent statistical potentials.
P2860
Q21090574-0C6B1406-AFBB-4C3A-A616-DDEF415A4DCDQ24817209-2118E4B2-5295-4103-9F6B-5A196B576209Q27622724-0CAF7F3F-5D66-4D30-9485-7A1C262A1F93Q27637748-E6741A24-9B3A-43AB-82CE-4AC302A2428BQ27639831-724966E8-E05A-4261-87BE-A11967090D90Q27639875-E6726E17-5ECB-4285-AF7A-8E035E958409Q27640129-40A5709F-CE7E-4B22-85D0-B1054292BD17Q27641507-EAFE0FAC-9E1E-49CD-BA4B-67E0CEDE7D6CQ27641604-C425CB8B-892D-45F3-BE11-2BC0B73C9BBAQ27650393-D6C98187-8168-4FFE-8320-99AFE5B6274AQ27653144-9132244F-3AB6-40EC-ADFC-8584279527B7Q27653471-3653AC3E-B90C-4F12-BC52-5500D002D626Q27656008-990C9684-E472-4F80-89CD-E25D6FBF61A3Q27670631-3D58BD03-630C-4175-8753-CF58B137E488Q27680992-A0BA0B92-7419-4FEC-9EA7-A087A48D50D8Q27682720-B1BE7579-243E-46E7-A8C1-D690204559C6Q27702871-7C7EB44B-B8AA-423B-8284-E5EB33C5920CQ28203641-ED2697F2-EED8-4809-AAEB-E55E78D50FFCQ28365668-2F6385C8-9940-480E-BD5A-DCCED06F9C88Q28483556-205B21E9-3FB2-4F5F-BC98-138B9AFCE428Q28730148-8EBBC0B7-EB75-4BD5-BBB4-CD30D3E2F9B4Q30326371-78DFA37A-FA96-4C4A-B7C5-0F07F40FBF46Q30342632-640992DB-4B47-43F5-BFA9-288F6A4C1810Q30416939-151CDC1E-4A24-40F2-8990-9EFB6FAA9DC8Q30884013-E10351F2-C0F2-495A-8A4B-5C56E2883A99Q31030886-F77F5703-01F8-427D-8517-793F253E9DD9Q33195739-5F44EF77-2C82-44E0-8D3B-384B96B3C542Q33281933-9D80F5BD-057F-4F5C-8EA8-32C68FA3022AQ33321952-312F2AC7-6F85-4731-B773-B7DD60DD77CEQ33582647-E14997C0-AC87-4C7C-A7E1-AF1982343EA9Q33782649-F8148532-A2B6-47BE-801B-457C115C55EAQ33993711-556E43E0-86BA-46C4-B44F-A42A1640031AQ34018164-95C4AD3D-76E7-4006-80CF-55FD539E3DD3Q34100973-E191A742-14BC-457D-97BA-0F21392BA951Q34178635-6F6B7C62-6B86-4880-A9FF-9E27943E3F56Q34178725-A10273A4-E361-4C7E-9467-D0CF0F82ED2AQ34179334-A995A586-B2AD-4427-83F3-453BF1CB02AAQ34183601-12BC58CF-A8FF-400D-93DF-E99307BE8C3CQ35107288-12C5F0D0-039B-4A7A-B399-98D8D95D7B87Q35124961-DE4A76B5-D678-4D8C-B369-536275B4F13C
P2860
The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
The stability of salt bridges ...... or hyperthermophilic proteins.
@en
The stability of salt bridges ...... or hyperthermophilic proteins.
@nl
type
label
The stability of salt bridges ...... or hyperthermophilic proteins.
@en
The stability of salt bridges ...... or hyperthermophilic proteins.
@nl
prefLabel
The stability of salt bridges ...... or hyperthermophilic proteins.
@en
The stability of salt bridges ...... or hyperthermophilic proteins.
@nl
P356
P1476
The stability of salt bridges ...... or hyperthermophilic proteins.
@en
P2093
P304
P356
10.1006/JMBI.1998.2159
P407
P577
1998-11-01T00:00:00Z