Search results for "Biophysical methods"

showing 2 items of 2 documents

Precision and accuracy of single-molecule FRET measurements-a multi-laboratory benchmark study

2018

Single-molecule Forster resonance energy transfer (smFRET) is increasingly being used to determine distances, structures, and dynamics of biomolecules in vitro and in vivo. However, generalized protocols and FRET standards to ensure the reproducibility and accuracy of measurements of FRET efficiencies are currently lacking. Here we report the results of a comparative blind study in which 20 labs determined the FRET efficiencies (E) of several dye-labeled DNA duplexes. Using a unified, straightforward method, we obtained FRET efficiencies with s.d. between +/- 0.02 and +/- 0.05. We suggest experimental and computational procedures for converting FRET efficiencies into accurate distances, and…

0301 basic medicinePHOTON DISTRIBUTIONDYNAMICSAccuracy and precisionTechnologyBiophysicsRESONANCE ENERGY-TRANSFERBiochemistryMedical and Health SciencesArticle03 medical and health sciencesBlind studySingle-molecule biophysicsALTERNATING-LASER EXCITATIONSTRUCTURAL INFORMATIONFluorescence resonance energy transferDEPENDENCEQuantitative assessmentLife ScienceFLUORESCENCEStructure determinationMolecular BiologyQCVLAGBiophysical methodsReproducibilityReproducibility of ResultsCell BiologySingle-molecule FRETDNABiological SciencesPublisher CorrectionQPSPECTROSCOPIC RULER030104 developmental biologyFörster resonance energy transferBiofysicaBenchmark (computing)Photon distributionEPSREFRACTIVE-INDEXLaboratoriesBiological systemBiotechnologyDevelopmental Biology
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Biophysical approaches for the study of metal-protein interactions

2019

Protein-protein interactions play important roles for a variety of cell functions, often involving metal ions; in fact, metal-ion binding mediates and regulates the activity of a wide range of biomolecules. Enlightening all of the specific features of metal-protein and metal-mediated protein-protein interactions can be a very challenging task; a detailed knowledge of the thermodynamic and spectroscopic parameters and the structural changes of the protein is normally required. For this purpose, many experimental techniques are employed, embracing all fields of Analytical and Bioinorganic Chemistry. In addition, the use of peptide models, reproducing the primary sequence of the metal-binding …

chemistry.chemical_classificationBiophysical methodsBinding Sites010405 organic chemistryChemistryBiomoleculeMetal-protein interactionsStructural and kinetic toolsProteinsComputational biologyAnalytical techniques010402 general chemistry01 natural sciencesBiochemistryCell function0104 chemical sciencesProtein–protein interactionInorganic ChemistryKineticsMetalsPeptidesPrimary sequenceProtein BindingJournal of Inorganic Biochemistry
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