Blar i Department of Biological Sciences på forfatter "Khan, Hanif Muhammad"
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Cation‐π Interactions between Methylated Ammonium Groups and Tryptophan in the CHARMM36 Additive Force Field
Khan, Hanif Muhammad; MacKerell, Alexander D.; Reuter, Nathalie (Peer reviewed; Journal article, 2019)Cation-π interactions between tryptophan and choline or trimethylated lysines are vital for many biological processes. The performance of the additive CHARMM36 force field against target quantum mechanical data is shown ... -
A Role for Weak Electrostatic Interactions in Peripheral Membrane Protein Binding
Khan, Hanif Muhammad; He, Tao; Fuglebakk, Edvin; Grauffel, Cédric; Yang, Boqian; Roberts, Mary F.; Gershenson, Anne; Reuter, Nathalie (Peer reviewed; Journal article, 2016-03)Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (BtPI-PLC) is a secreted virulence factor that binds specifically to phosphatidylcholine (PC) bilayers containing negatively charged phospholipids. ... -
Role of noncovalent interactions in protein peripheral membrane binding. Computational perspectives
Khan, Hanif Muhammad (Doctoral thesis, 2016-02-19)Noncovalent forces are important driving forces in nature particularly in biology, and they dictate many biological processes including the binding of peripheral protein to the cell membrane. The widely acknowledged models ... -
Standard Binding Free Energy and Membrane Desorption Mechanism for a Phospholipase C
Moutoussamy, Emmanuel Edouard; Khan, Hanif Muhammad; Roberts, Mary B; Gershenson, Anne; Chipot, Christophe; Reuter, Nathalie (Journal article; Peer reviewed, 2022)Peripheral membrane proteins (PMPs) bind temporarily to cellular membranes and play important roles in signaling, lipid metabolism, and membrane trafficking. Obtaining accurate membrane-PMP affinities using experimental ... -
Two homologous neutrophil serine proteases bind to POPC vesicles with different affinities: When aromatic amino acids matter
Schillinger, Anne-Sophie; Grauffel, Cédric; Khan, Hanif Muhammad; Halskau, Øyvind; Reuter, Nathalie (Peer reviewed; Journal article, 2014-12)Neutrophil serine proteases Proteinase 3 (PR3) and human neutrophil elastase (HNE) are homologous antibiotic serine proteases of the polymorphonuclear neutrophils. Despite sharing a 56% sequence identity they have been ...