Studies of the function of membrane and soluble proteins and their biophysical properties.

NIH RePORTER · NIH · R35 · $419,639 · view on reporter.nih.gov ↗

Abstract

Over the past 50 years, the field of biophysical chemistry has learned an enormous amount about the relationships between the function, dynamics and folding of soluble proteins. The next stage in biological science involves addressing more complex problems on more challenging systems using increasingly sophisticated approaches augmented by computational methods. The Sosnick lab has followed this path. We are conducting studies of membrane proteins, condensates and disordered proteins. Our ability to address these topics arises in part from our expertise in the folding of soluble and more recently, membrane proteins. We build on this experience and knowledge to advance new or improve existing methods. The proposed research relies heavily on hydrogen exchange (HX), a method developed to study folding and dynamics yet possessing broad transferability to many methods. We plan to continue this approach and study the metabolite transport across a bilayer, stress-induced phase separation, and properties of disordered proteins in addition to membrane protein folding. Many of the projects are collaborative, leveraging our skills and interests with those of other labs, which further supports the value of our studies.

Key facts

NIH application ID
10552333
Project number
1R35GM148233-01
Recipient
UNIVERSITY OF CHICAGO
Principal Investigator
Tobin R Sosnick
Activity code
R35
Funding institute
NIH
Fiscal year
2023
Award amount
$419,639
Award type
1
Project period
2023-03-01 → 2028-02-29