There are inherent limitations with traditional methods to study protein behavior or to determine the constituency of proteins in discrete subcellular compartments.
Current methods to study protein structure are very interesting to discover enzymes with improved catalytic properties and activities [ 19].
An exception is the use of pulsed field gradient methods to study protein diffusion [ 87] but this has not yet been used in studies of proteins within liquid-like droplets.
Our lab and others have been developing SDFL methods that exploit the small size and excellent spectral properties of the fluorophore bimane, with the goal of improving the resolution and ability of SDFL methods to study protein structure and dynamics.
The study of histone glycosylation is still in its infancy, but advanced methods to study protein glycosylation may be borrowed from other fields of research, and highly complex glycopeptides and glycoproteins can be synthesized.
Together, our data highlight unique aspects of using Tyr as a quencher and demonstrate how a combined use of TrIQ and TyrIQ in parallel significantly enhances the resolution and ability of these SDFL methods to study protein dynamics and energetics.
It may be expected that with further advancement of mass spectrometric analysis, stable isotopes will offer alternative methods to study protein turnover also for eukaryotic multicellular organisms similar to unicellular organisms that can easily be labelled in suspension [ 32].
This electrochemical method is simple, which may provide a novel method to study protein modifications in the future.
Until now the PET-labeled amino acids have mostly been applied to measure protein synthesis in tumors or in cerebrum and only few studies have applied the method to study protein synthesis in skeletal muscle.
Far-UV circular dichroism (CD) is a common method to study protein secondary structure because different types of regular secondary structure found in proteins give rise to characteristic CD spectra in the far UV region.
