Open Access. Powered by Scholars. Published by Universities.®
Biological and Chemical Physics Commons™
Open Access. Powered by Scholars. Published by Universities.®
- Keyword
-
- Aromatic disulfides (1)
- Aromatic thiols (1)
- BPTI (1)
- Biomolecular interactions (1)
- Carbon nanotube based nanoporous membrane devices (1)
-
- Conformational folding (1)
- DNA supercoiling (1)
- DNA topoisomerases (1)
- Finite element simulations (1)
- Glutathione (GSH) (1)
- Glutathione disulfide (GSSG) (1)
- HPLC (1)
- Heme proteins (1)
- Label-free methods (1)
- Molecular dynamics (MD) (1)
- Protein folding (1)
- Quartz nanopipettes (1)
- SPR data fitting (1)
- Surface plasmon resonance (SPR) (1)
- Targeted MD (TMD) (1)
Articles 1 - 2 of 2
Full-Text Articles in Biological and Chemical Physics
Folding Of Bovine Pancreatic Trypsin Inhibitor (Bpti) Is Faster Using Aromatic Thiols And Their Corresponding Disulfides, Ram Prasad Marahatta
Folding Of Bovine Pancreatic Trypsin Inhibitor (Bpti) Is Faster Using Aromatic Thiols And Their Corresponding Disulfides, Ram Prasad Marahatta
FIU Electronic Theses and Dissertations
Improvement in the in vitro oxidative folding of disulfide-containing proteins, such as extracellular and pharmaceutically important proteins, is required. Traditional folding methods using small molecule aliphatic thiol and disulfide, such as glutathione (GSH) and glutathione disulfide (GSSG) are slow and low yielding. Small molecule aromatic thiols and disulfides show great potentiality because aromatic thiols have low pKa values, close to the thiol pKa of protein disulfide isomerase (PDI), higher nucleophilicity and good leaving group ability. Our studies showed that thiols with a positively charged group, quaternary ammonium salts (QAS), are better than thiols with negatively charged groups such as phosphonic …
Multimode Analysis Of Nanoscale Biomolecular Interactions, Purushottam Babu Tiwari
Multimode Analysis Of Nanoscale Biomolecular Interactions, Purushottam Babu Tiwari
FIU Electronic Theses and Dissertations
Biomolecular interactions, including protein-protein, protein-DNA, and protein-ligand interactions, are of special importance in all biological systems. These interactions may occer during the loading of biomolecules to interfaces, the translocation of biomolecules through transmembrane protein pores, and the movement of biomolecules in a crowded intracellular environment. The molecular interaction of a protein with its binding partners is crucial in fundamental biological processes such as electron transfer, intracellular signal transmission and regulation, neuroprotective mechanisms, and regulation of DNA topology. In this dissertation, a customized surface plasmon resonance (SPR) has been optimized and new theoretical and label free experimental methods with related analytical …