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Articles by Martin D. Gelenter
Recombinant Expression and Chemical Amidation of Isotopically Labeled Native Melittin
Post-translational modifications are ubiquitous in the eukaryotic proteome. However, these modifications are rarely incorporated in NMR studies of eukaryotic proteins, which are typically produced through recombinant expression in . Melittin is the primary peptide in honey bee venom. Its native C-terminal amide significantly affects its equilibrium structure and dynamics in solution and is thus a prerequisite for studying its native structure and function.
Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range 13C-13C and 15N-13C Distance Restraints
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Phys. Chem. B 2020, XXXX, XXX RETURN TO JUST ACCEPTED MANUSCRIPTSPREVB: Biophysics; Physi...B: Biophysics; Physical Chemistry of Biological Systems and BiomoleculesNEXT Martin D. Gelenter, Aurelio J. Dregni, and Mei Hong LEARN ABOUT THESE METRICS Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals.
The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations
Abstract Glucagon and insulin maintain blood glucose homeostasis and are used to treat hypoglycemia and hyperglycemia, respectively, in patients with diabetes. Whereas insulin is stable for weeks in its solution formulation, glucagon fibrillizes rapidly at the acidic pH required for solubility and is therefore formulated as a lyophilized powder that is reconstituted in an acidic solution immediately before use.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR - Journal of the American Chemical Society (ACS Publications)
The influenza M2 protein forms a tetrameric proton channel that conducts protons from the acidic endosome into the virion by shuttling protons between water and a transmembrane histidine. Previous NMR studies have shown that this histidine protonates and deprotonates on the microsecond time scale. However, M2’s proton conduction rate is 10–1000 s–1, more than 2 orders of magnitude slower than the histidine-water proton-exchange rate. M2 is also known to be conformationally plastic.
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