Role of aromatic localization in the gating process of a potassium channel.
|Abstract||Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for transmembrane aromatic residues to reside at the interfaces. The process of aromatic localization is proposed as a means of directing and stabilizing st ... [truncated at 450 characters in length]|
|Author||Domene, Carmen; Vemparala, Satyavani; Klein, Michael L; et al|
|Subject||Biophysics Cell Membrane Computer Simulation G Protein-Coupled Inwardly-Rectifying Potassium Channels Ion Channel Gating Lipid Bilayers Lipids Models, Molecular Molecular Conformation Phenylalanine Potassium Channels Time Factors Tyrosine methods metabolism chemistry chemistry chemistry chemistry chemistry chemistry|
Structure-activity relationships among the nitrogen containing bisphosphonates in clinical use and other analogues: time-dependent inhibition of human farnesyl pyrophosphate synthase.
|Abstract||The nitrogen-containing bisphosphonates (N-BPs) are the main drugs currently used to treat diseases characterized by excessive bone resorption. The major molecular target of N-BPs is farnesylpyrophosphate synthase. N-BPs inhibit the enzyme by a mechanism that involves time dependent isomerization of the enzyme. We investigated features of N-BPs that confer maximal slow and tight-binding by quantifying the initial and final K(i)s and calculating t ... [truncated at 450 characters in length]|
|Author||Dunford, James E; Kwaasi, Aaron A; Rogers, Michael J; et al|
|Subject||Binding Sites Diphosphonates Enzyme Inhibitors Geranyltranstransferase Humans Models, Molecular Molecular Structure Nitrogen Stereoisomerism Structure-Activity Relationship Time Factors chemistry pharmacology chemistry pharmacology antagonists and inhibitors chemistry|