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Dynamic Properties that Enhance Enzyme Function

Dynamic Properties that Enhance Enzyme Function
增强酶功能的动态特性
批准号：
8450124
负责人：
Sidney M. Hecht
金额：
$30.1万
依托单位：
ARIZONA STATE UNIVERSITY-TEMPE CAMPUS
依托单位国家：
美国
项目类别：
财政年份：
2010
资助国家：
美国
项目状态：
已结题
起止时间：
2010-04-01 至 2015-03-31
来源：
https://reporter.nih.gov/project-details/8450124
关键词：
AcidsActive SitesAddressAllosteric RegulationAmino AcidsAntineoplastic AgentsBehaviorBindingBiochemical ReactionCatalysisCharacteristicsChemicalsCoupledCouplingDevelopmentDihydrofolate ReductaseDistantEnvironmentEnzymesEventEvolutionFluorescence SpectroscopyFluorescent ProbesFosteringFreedomFrequenciesGoalsInvestigationKineticsKnowledgeLabelLaboratoriesLeadMapsMediatingMethodologyMethodsModificationMotionNMR SpectroscopyNaturePhysiologicalPlayPost-Translational Protein ProcessingProcessPropertyProtein DynamicsProtein SubunitsProteinsPublishingReactionResearchResolutionRoleSideSiteSolutionsSolventsStructureSystemTertiary Protein StructureTimeVertebral columnWorkX-Ray Crystallographyantimicrobial drugbasecofactordesigndrug discoveryenzyme mechanismenzyme substrate complexflexibilityfluorophoreimprovedinsightnoveloperationprotein foldingprotein functionprotein structureprotein structure functionpublic health relevanceresearch and developmentsingle moleculethree dimensional structuretool

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中文摘要
翻译
描述（由申请人提供）：本研究的长期目标包括发展研究蛋白质结构的折叠、灵活性和动力学的方法，以及开发和使用荧光探针的新方法，以增强我们对蛋白质结构、动力学和功能的理解。在拟建的5年研究期内，将重点通过稳态、预稳态和单分子动力学研究对改性DHFRs的机理进行研究。荧光光谱将用于研究蛋白质的构象变化及其与DHFR催化关键步骤的关系。
英文摘要
DESCRIPTION (provided by applicant): The long term goals of this research include the development of methodology to permit the folding, flexibility and dynamics of protein structure to be interrogated, and the development and use of fluorescent probes in novel ways to enhance our understanding of protein structure, dynamics and function. During the five years of proposed research, the focus of efforts will be on study of the mechanism of modified DHFRs through steady state, pre-steady state and single molecule kinetic studies. Fluorescence spectroscopy will be used to study the protein conformational changes and their association with the key steps in DHFR catalysis.
期刊论文(8)
专著(0)
科研奖励(0)
会议论文
Tryptophan-based fluorophores for studying protein conformational changes.
DOI： 10.1016/j.bmc.2014.09.015
发表时间： 2014-11-01
期刊： Bioorganic & medicinal chemistry
影响因子： 3.5
作者： [Talukder P, Chen S, Liu CT, Baldwin EA, Benkovic SJ, Hecht SM]
通讯作者： Hecht SM
Efficient asymmetric synthesis of tryptophan analogues having useful photophysical properties.
DOI： 10.1021/ol403429e
发表时间： 2014-01-17
期刊： ORGANIC LETTERS
影响因子： 5.2
作者： [Talukder, Poulami, Chen, Shengxi, Arce, Pablo M., Hecht, Sidney M.]
通讯作者： Hecht, Sidney M.
Two pyrenylalanines in dihydrofolate reductase form an excimer enabling the study of protein dynamics.
DOI： 10.1021/ja307179q
发表时间： 2012-11-21
期刊： Journal of the American Chemical Society
影响因子： 15
作者： [Chen S, Wang L, Fahmi NE, Benkovic SJ, Hecht SM]
通讯作者： Hecht SM
The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.
活性位点异亮氨酸至丙氨酸突变对 DHFR 催化氢化物转移的影响。
DOI： 10.1039/c0cc02988b
发表时间： 2010
期刊： Chemical communications (Cambridge, England)
影响因子： --
作者： [Stojković,Vanja, Perissinotti,LauraL, Lee,Jeeyeon, Benkovic,StephenJ, Kohen,Amnon]
通讯作者： Kohen,Amnon
Biological Regulation Studied In Vitro and In Cellulo with Modified Proteins
Biological Regulation Studied In Vitro and In Cellulo with Modified Proteins
Biological Regulation Studied In Vitro and In Cellulo with Modified Proteins
Ribosomally Synthesized Proteins Incorporating Modified Dipeptides
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