Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsion
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Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRETThe effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contextsElectron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin.Calmodulin transduces Ca2+ oscillations into differential regulation of its target proteinsA Microfluidic Platform for Real-Time Detection and Quantification of Protein-Ligand Interactions.Life under the Microscope: Single-Molecule Fluorescence Highlights the RNA World.
P2860
Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsion
description
im April 2013 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2013
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name
Förster resonance energy trans ...... domain electrostatic repulsion
@en
Förster resonance energy trans ...... domain electrostatic repulsion
@nl
type
label
Förster resonance energy trans ...... domain electrostatic repulsion
@en
Förster resonance energy trans ...... domain electrostatic repulsion
@nl
prefLabel
Förster resonance energy trans ...... domain electrostatic repulsion
@en
Förster resonance energy trans ...... domain electrostatic repulsion
@nl
P2093
P2860
P356
P1433
P1476
Förster resonance energy trans ...... domain electrostatic repulsion
@en
P2093
Anita Kohli
Beth Krouse
Cynthia F. Shuman
Erik Hellstrand
Eva Thulin
Karin S. Åkerfeldt
Sara Steenbergen
Stephanie Kukora
P2860
P304
P356
10.1111/FEBS.12269
P407
P577
2013-04-29T00:00:00Z