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Investigations of Protein Folding by Solid State NMR

Investigations of Protein Folding by Solid State NMR
通过固态核磁共振研究蛋白质折叠
批准号：
8349713
负责人：
ROBERT TYCKO
金额：
$15.9万
依托单位：
NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
依托单位国家：
美国
项目类别：
财政年份：
--
资助国家：
美国
项目状态：
未结题
起止时间：
至
来源：
https://reporter.nih.gov/project-details/8349713
关键词：
AddressAmyloid FibrilsBiological ProcessChemicalsCollaborationsComputer SimulationCrystallographyDataDependenceDevelopmentDiseaseEquilibriumFreezingGlassGoalsInvestigationKineticsLabelLaboratoriesMagicMeasurementMeasuresMethodsModelingOpticsPlayProcessPropertyProteinsPublishingRelative (related person)RelaxationResolutionRoleSamplingSiteSolutionsSolventsSpectrum AnalysisStructural ModelsStructureSystemTechniquesTechnologyThermodynamicscold temperatureirradiationmicrowave electromagnetic radiationprotein foldingresearch studysolid state nuclear magnetic resonance

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中文摘要
翻译
二零一一财政年度并无进行新的蛋白质折叠实验。 然而，大量的努力致力于开发新的固态NMR技术，这将使实验在2012财政年度，特别是一个新的低温魔角旋转探针与微波辐射能力，将提高蛋白质折叠测量的灵敏度至少50倍，相对于我们以前发表的结果。 此外，我们还与维克托穆尼奥斯教授合作，使用2011财年和前几年在我们实验室合成的同位素标记蛋白质样品，测量和解释热解折叠HP 35的溶液NMR化学位移和弛豫参数。
英文摘要
No new protein folding experiments were performed in FY2011. However, much effort was devoted to the development of new solid state NMR technology that will enable experiments in FY2012, particularly a new low-temperature magic-angle spinning probe with microwave irradiation capabilities that will enhance the sensitivity of protein folding measurements by a factor of at least 50 relative to our previously published results. In addition, we have initiated a collaboration with Prof. Victor Munoz to measure and interpret solution NMR chemical shifts and relaxation parameters in thermally unfolded HP35, using isotopically labeled protein samples that were synthesized in our laboratory in FY2011 and previous years.
期刊论文(3)
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会议论文
What can solid state NMR contribute to our understanding of protein folding?
DOI： 10.1016/j.bpc.2010.05.009
发表时间： 2010-09
期刊： BIOPHYSICAL CHEMISTRY
影响因子： 3.8
作者： [Hu, Kan-Nian, Tycko, Robert]
通讯作者： Tycko, Robert
Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.
DOI： 10.1016/j.jmb.2009.07.073
发表时间： 2009-10-02
期刊： JOURNAL OF MOLECULAR BIOLOGY
影响因子： 5.6
作者： [Hu, Kan-Nian, Havlin, Robert H., Yau, Wai-Ming, Tycko, Robert]
通讯作者： Tycko, Robert
Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance.
DOI： 10.1021/ja908471n
发表时间： 2010-01-13
期刊： JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
影响因子： 15
作者： [Hu, Kan-Nian, Yau, Wai-Ming, Tycko, Robert]
通讯作者： Tycko, Robert
NEW SOLID STATE NMR METHODOLOGY FOR STRUCTURAL STUDIES OF BIOPOLYMERS
Structural Studies of Prion Fibrils and Other Protein Fibrils
Development of Solid State NMR Methods and Technology
Development of Solid State NMR Methods and Technology
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