Related Experiment Video
Updated: Aug 14, 2026

11:55
Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Dynamics of formation of a helix-turn-helix structure in a membrane-active peptide: a time-resolved spectroscopic
Mariano Venanzi1, Emanuela Gatto, Gianfranco Bocchinfuso
1Department of Sciences and Chemical Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy. venanzi@uniroma2.it
Chembiochem : a European Journal of Chemical Biology
|November 25, 2005
Abstract
No abstract available in PubMed .
More Related Videos
Related Concept Videos
Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

