Return to search

Diffusion detects conformation changes during reactions of photosensor proteins

Since conformation changes of proteins and biomolecular interactions (including protein-DNA, or
protein-protein interactions) are essential processes for biological functions, detections of these
processes are important in chemistry and biochemistry to understand the reactions. For the detection of
these processes, a variety of techniques have been developed. UV/vis absorption spectroscopy or
emission spectroscopy are very powerful to trace the time development of reactions. However, these
techniques have a limitation to detect the conformation changes of proteins and biomolecular
interactions. Recently, our group discovered that the translational diffusion coefficient can be a useful
and sensitive probe to detect the conformation change as well as the intermolecular interaction changes.
Although many techniques, e.g., dynamic light scattering, Taylor dispersion, capillary method, NMR
spectroscopy, have been developed to monitor molecular diffusion, molecular diffusion has never been
considered as a time dependent property during reactions. We have been developing a method based on
the pulsed-laser induced transient grating (TG) technique to detect the time-dependent diffusion. Here,
we repot the time-resolved detection of protein conformation changes of a blue light sensor protein of
phototropin by using the diffusion coefficient.

Identiferoai:union.ndltd.org:DRESDEN/oai:qucosa:de:qucosa:38267
Date06 February 2020
CreatorsTerazima, Masahide, Nakasone, Yusuke
Source SetsHochschulschriftenserver (HSSS) der SLUB Dresden
LanguageEnglish
Detected LanguageEnglish
Typeinfo:eu-repo/semantics/acceptedVersion, doc-type:article, info:eu-repo/semantics/article, doc-type:Text
Rightsinfo:eu-repo/semantics/openAccess
Relation26, urn:nbn:de:bsz:15-qucosa2-378382, qucosa:37838

Page generated in 0.0018 seconds