Publications by authors named "Laila M R Singh"
Article Synopsis
- - Heme-copper oxidases (HCuOs) play a crucial role in the respiratory chain, facilitating the reduction of oxygen to water and generating a proton-motive force, essential for energy production in both mitochondria and certain bacteria.
- - Cbb3-type heme-copper oxidases, primarily found in pathogenic bacteria, have low affinity for oxygen, allowing them to thrive in low-oxygen environments, and display significant structural differences from mitochondrial-like oxidases that affect their function and ligand binding.
- - Recent studies reveal how binding of carbon monoxide (CO) to cbb3 oxidases can be influenced by protein-lipid interactions in the membrane, and these findings could provide insights into the physiological roles of these interactions in
Amphitropic proteins are regulated by reversible membrane interaction. Anionic phospholipids generally promote membrane binding of such proteins via electrostatics between the negatively charged lipid headgroups and clusters of basic groups on the proteins. In this study of one amphitropic protein, a cytidylyltransferase (CT) that regulates phosphatidylcholine synthesis, we found that substitution of lysines to glutamine along both interfacial strips of the membrane-binding amphipathic helix eliminated electrostatic binding.
View Article and Find Full Text PDFAmide hydrogen/deuterium exchange rates were measured as a function of pH and urea for 37 slowly exchanging amides in the beta-trefoil protein hisactophilin. The rank order of exchange rates is generally maintained under different solution conditions, and trends in the pH and urea dependence of exchange rates are correlated with the rank order of exchange rates. The observed trends are consistent with the expected behavior for exchange of different amides via global and/or local unfolding.
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