A5078435702- Heat shock proteins research
- Toxin Mechanisms and Immunotoxins
- Enzyme Structure and Function
- Microfluidic and Bio-sensing Technologies
- Enzyme Production and Characterization
- Supramolecular Self-Assembly in Materials
- RNA Interference and Gene Delivery
- 3D Printing in Biomedical Research
- Erythrocyte Function and Pathophysiology
- Endoplasmic Reticulum Stress and Disease
- Protein Structure and Dynamics
- Nanoplatforms for cancer theranostics
University of Pittsburgh
2023
Indian Institute of Technology Delhi
2015-2018
Transmembrane proteins have unique requirements to fold and integrate into the endoplasmic reticulum (ER) membrane. Most notably, transmembrane must in three separate environments: extracellular domains oxidizing environment of ER lumen, (TMDs) within lipid bilayer, cytosolic reducing cytosol. Moreover, each region is acted upon by a set chaperones monitored components associated quality control machinery that identify misfolded compartment. One factor lumenal Hsp70-like chaperone, Lhs1. Our...
Protein folding has been extensively studied for the past six decades by employing solution-based methods such as solubility, enzymatic activity, secondary structure analysis, and analytical like FRET, NMR, HD exchange. However, rapid analysis of process, approaches are often plagued with aggregation side reactions resulting in poor yields. In this work, we demonstrate that a bio-layer interferometry (BLI) chaperonin detection system can identify superior refolding conditions denatured...