POWRE: Solid State NMR Studies of Oligomerization: Zippering B-Strands from E. Coli Thioredoxin

Cuny City College, New York NY

Investigators

Abstract

Tasayco 0075115 The objective of this research is to establish the principles underlying oligomerization of disordered polypeptide chains through the zippering of b strands. Fragments of oxidized E. coli thioredoxin, a single domain a /b proteins of 108 residues well studied by fragment complementation, provide a unique opportunity to study oligomerization in the absence of the fully complementary fragment. The fragment 1-37 self assembles to produce large molecular weight homo-oligomers, and also interacts with fragment 74-108 to form hetero-oligomers. These homo and hetero-oligomers will be examined using recently developed solid-state nuclear magnetic resonance (SSNMR) methods, as well as complementary biochemical and biophysical standard techniques to determine the topology. Solid state nuclear magnetic resonance methodologies are a powerful tool for detailed structural analysis of oligomers. This is a POWRE proposal, for the PI, a leader in studying protein recognition by fragment complementation, to collaborate with a colleague in a nearby institution who is experienced in SSNMR, and to learn these techniques.