Publications by authors named "Nazmul H Khan"
Article Synopsis
- Membrane proteins, like inward-rectifier K (Kir) channels, have evolved alongside lipids to create complex activation mechanisms, influenced by specific lipids and water accessibility.
- The study focused on mutations in the KirBac1.1 channel, revealing that certain mutations dramatically reduced channel activity by affecting lipid-protein interactions and water accessibility.
- Results indicate that lipid binding triggers significant changes in the configuration of the protein, enhancing water access to the potassium conduction pathway, emphasizing the importance of lipid and water interactions in membrane protein functionality.
Maturation of the functional mouse CRES amyloid from globular form.
Proc Natl Acad Sci U S A
July 2020
Article Synopsis
- The study investigates the assembly of functional amyloids in the epididymal lumen, focusing on a cystatin-rich matrix that aids in sperm maturation and protection.
- Researchers developed a purification protocol for a mouse protein called CRES, using advanced techniques like X-ray crystallography and NMR to observe its transition from a single protein unit to a complex amyloid structure.
- Findings reveal that CRES monomers have a distinct structural fold and can assemble through two mechanisms, providing insights into how functional amyloids form and emphasizing their diverse assembly processes.
Article Synopsis
- The study investigates how lipid binding affects the structural changes necessary for activation and potassium (K) conduction in inward-rectifier K (Kir) channels, particularly in the prokaryotic KirBac1.1, which is similar to human Kir channels.
- Researchers found that KirBac1.1 is continually active when reconstituted in a mixture of specific lipids (POPC:POPG), using techniques like fluorescence quenching and Förster resonance energy transfer (FRET) to measure changes.
- Solid-state NMR spectroscopy revealed two different conformations of the channel in the activating lipid environment, indicating complex allosteric pathways and interactions between various structural components that drive the channel's activation, with specific
Article Synopsis
- An amyloid matrix with family 2 cystatins, notably the reproductive cystatin CRES, is essential for sperm maturation and protection in the mouse epididymal lumen.
- Research focused on purifying CRES to study its aggregation from a single unit to amyloid under conditions mimicking those in the epididymis.
- Unlike most amyloids, CRES forms unique antiparallel β-sheet-rich structures and its early oligomers might play a crucial role in assembling functional amyloids.
The hydrolysis of β-lactam antibiotics by β-lactamase enzymes is the most prominent antibiotic resistance mechanism for many pathogenic bacteria. Out of this broad class of enzymes, metallo-β-lactamases are of special clinical interest because of their broad substrate specificities. Several in vitro inhibitors for various metallo-β-lactamases have been reported with no clinical efficacy.
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