New methodologies for measuring protein interactions in vivo and in vitro.
The identification and characterization of protein interactions is a key topic in current life science research; a huge variety of methodologies have been established in recent years to expedite research in this area. Generic methods have been established for monitoring protein interactions in vivo by protein fragment complementation and for screening protein interactions in vitro by highly parallel solid-phase techniques. Substantial progress has been made in identifying and characterizing interactions with and between membrane proteins. Studying protein interactions on the single-molecule level has become an important tool for understanding protein function in vivo and in vitro.
Piehler
Jacob
J
Institute of Biochemistry, Biocenter N210, Johann Wolfgang Goethe-University, Marie-Curie Strasse 9, 60439 Frankfurt am Main, Germany. j.piehler@em.uni-frankfurt.de
D031541:Fluorescence Resonance Energy Transfer / Q000295:instrumentation / Q000379:methods* / Q000639:trends; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods* / Q000639:trends; D015335:Molecular Probes; D040081:Protein Array Analysis / Q000295:instrumentation / Q000379:methods* / Q000639:trends; D025941:Protein Interaction Mapping / Q000379:methods*; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods* / Q000639:trends; D020798:Two-Hybrid System Techniques
D015335:Molecular Probes