User:Snowwhite5567/sandbox

Italics are my additions. I am rearranging and adding to the current "applications" section.

Applications

The applications of fluorescence resonance energy transfer (FRET) have expanded tremendously in the last 25 years, and the technique has become a staple technique in many biological and biophysical fields. FRET can be used as spectroscopic ruler to measure distance and detect molecular interactions in a number of systems and has applications in biology and biochemistry.[23]

Proteins

FRET is often used to detect and track interactions between proteins.[42][43] [44] [45] Additionally, FRET can be used to measure distances between domains in a single protein by tagging different regions of the proteins with fluorophores and measuring interaction/emission to determine distance. This provides information about protein conformation, including secondary structures and protein folding. [40][41] This extends to tracking functional changes in protein structure, such as conformational changes associated with myosin activity [Shih]. Applied in vivo, FRET has been used to detect the location and interactions of cellular structures such as integrins and membrane proteins.[46]

Membranes

FRET can be used to observe membrane fluidity, movement and dispersal of membrane proteins, membrane lipid-protein and protein-protein interactions, and successful mixing of different membranes [Loura]. FRET is also used to study formation and properties of membrane domains and [Loura] lipid rafts in cell membranes [48] and to determine surface density in membranes.[49]

Chemosensory

FRET-based probe that activates with binding of Cd2+

FRET-based probes can detect the presence of various molecules: the probe’s structure is affected by small molecule binding or activity, which can turn the FRET system on or off. This is often used to detect anions, cations, small uncharged molecules, and some larger macromolecules as well. Similarly, FRET systems have been designed to detect changes in the cellular environment due to such factors as pH, hypoxia, or mitochondrial membrane potential [Wu].

Signaling pathways

Another use for FRET is in the study of metabolic or signaling pathways.[47] For example, FRET and BRET have been used in various experiments to characterize G-protein coupled receptor activation and consequent signaling pathways [Lohse]. Other examples include the use of FRET to analyze such diverse processes as caspase activity in apoptosis [Wu different one] and bacterial chemotaxis [Sourjik].

Other

In addition to common uses previously mentioned, FRET and BRET are also effective in the study of biochemical reaction kinetics [Liu]. FRET is increasingly used for monitoring pH dependent assembly and disassembly and is valuable in the analysis of nucleic acids.[54][55][56] This technique can be used to determine factors affecting various types of nanoparticle formation [52][53] as well as the mechanisms and effects of nanomedicines [Chen].