Publications by authors named "Megh R Bhatt"
Article Synopsis
- The type II polyproline helix (PPII) is a crucial protein structure influenced by n→π* interactions between carbonyl groups, which help stabilize this conformation.
- Research shows that varying the electronic properties of acyl capping groups can significantly affect the stability of PPII in peptides, with electron-rich groups (like pivaloyl and iso-butyryl) enhancing PPII formation compared to the standard acetyl group.
- Findings suggest that the choice of acyl capping groups should be carefully considered in peptide design, as they can greatly influence the structural properties of both proline and non-proline residues.
Article Synopsis
- * Peptides with different acyl groups showed that more electron-rich acyls (like pivaloyl and butyryl) actually destabilized α-helices, contrary to what was expected.
- * Both experimental and computational studies suggest that the interaction between water molecules and N-terminal amide groups plays a crucial role in determining the stability of α-helices.
Article Synopsis
- The chemical shifts of Dfp’s diastereotopic fluorines vary significantly based on whether proline is in an ordered or disordered state, providing insights into the preference of ring puckers, which indicate the stability of proline structures in peptides.
- Research utilizing Dfp revealed that the polyproline II helix formed in high urea has nearly equal populations of ring puckers and underscores the role of carbonyl solvation and specific
Article Synopsis
- Cysteine sulfonic acid (Cys-SOH; cysteic acid) is an irreversible oxidative modification of cysteine, indicating oxidative damage in proteins and acting as a biomarker for oxidative stress.
- The study utilized experimental methods, bioinformatics, and computational analysis to evaluate how Cys-SOH affects protein structure, specifically looking at its role in α-helix and polyproline II (PPII) helix formation.
- Solid-phase synthesis techniques using methyltrioxorhenium (MeReO) and hydrogensulfate generated peptides containing Cys-SOH efficiently, with findings showing varying impacts on the propensity for PPII and α-helix formations compared to neutral cysteine.
Article Synopsis
- * A series of proline derivatives were synthesized, showing close intermolecular C-H/O interactions in crystal structures, with some distances as small as 2.3 Å, indicating strong bonding.
- * Analysis of proline residues in various structures reveals that C-H/O interactions are prevalent and suggest that proline is vital for recognition and assembly in protein structures due to its unique hydrogen bonding characteristics.
Article Synopsis
- The study investigates how the preferred shapes of peptides and proteins are influenced by local interactions, specifically focusing on the n→π* interaction between adjacent carbonyls, which encourages more compact structures like α-helices.
- By synthesizing peptides with varied acyl groups and using techniques like NMR and X-ray crystallography, it was found that electron-rich acyl groups enhance n→π* interactions and lead to preferred α-helical conformations.
- The findings suggest that modifying acyl N-capping motifs could be a strategic approach to control peptide and protein structures in designing new molecules for medicinal chemistry.
Article Synopsis
- - Cytochrome b5 (cyt b5) is a small hemoprotein that enhances the activity of cytochrome P450 17α-hydroxylase/17,20-lyase (CYP17A1), an enzyme crucial for steroid hormone production.
- - Located in the adrenal cortex and gonads, CYP17A1 performs two key reactions, 17α-hydroxylation and 17,20-lyase, in the steroidogenesis pathway.
- - The review highlights how cyt b5 regulates CYP17A1, primarily by promoting its interaction with cytochrome P450 reductase (CPR) and serving as an electron donor to support its enzymatic activities.