14 results for "Harding, Benjamin D."
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Enhancing Spectrometer Performance with Unsupervised Machine Learning
Solid-state NMR spectroscopy (SSNMR) is a powerful technique to probe structural and dynamic properties of biomolecules at an atomic level. Modern SSNMR methods employ multidimensional pulse sequences requiring data collection over a period of days to weeks. Variations in signal intensity or…
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OPTO: Automated Optimization for Solid-State NMR Spectroscopy
NMR spectroscopy presents boundless opportunities for understanding structure, dynamics and function for a broad range of scientific applications. Solid-state NMR (SSNMR), in particular, provides novel insights into biological and materials systems that are not amenable to other approaches…
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Backbone and Sidechain (1)H, (15)N and (13)C Resonance Assignments of a Multidrug Efflux Membrane Protein using Solution and Solid-State NMR
EmrE is a bacterial membrane-embedded multidrug transporter that functions as an asymmetric homodimer. EmrE is implicated in antibiotic resistance, but is now known to confer either resistance or susceptibility depending on the identity of the small molecule substrate. Here, we report both…
Also available at: PubMed Central
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Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for protein structure determination, but traditional approaches require extensive manual assignment of hundreds to thousands of resonances. Here we present NMRFAM-BPHON, a novel “top-down” approach that treats experimental NMR…
Also available at: PubMed Central
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Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State
NMR structures of membrane proteins are often hampered by poor chemical shift dispersion and internal dynamics which limit resolved distance restraints. However, the ordering and topology of these systems can be defined with site-specific water or lipid proximity. Membrane protein water…
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Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies
Membrane proteins play an important role in maintaining the structure and physiology of an organism. Despite their significance, spectroscopic studies involving membrane proteins remain challenging due to the difficulties in mimicking their native lipid bilayer environment. Membrane mimetic systems…
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Characterization of the Human KCNQ1 Voltage Sensing Domain (VSD) in Lipodisq Nanoparticles for Electron Paramagnetic Resonance (EPR) Spectroscopic Studies of Membrane Proteins
Membrane proteins are responsible for conducting essential biological functions that are necessary for the survival of living organisms. In spite of their physiological importance, limited structural information is currently available as a result of challenges in applying biophysical techniques for…
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Cross polarization stability in multidimensional NMR spectroscopy of biological solids
Magic-angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) spectroscopy is a powerful and versatile technique for probing structure and dynamics in large, insoluble biological systems at atomic resolution. With many recent advances in instrumentation and polarization methods…
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Probing the Dynamics and Structural Topology of the Reconstituted Human KCNQ1 Voltage Sensor Domain (Q1-VSD) in Lipid Bilayers Using Electron Paramagnetic Resonance Spectroscopy
KCNQ1 (Kv7.1 or KvLQT1) is a potassium ion channel protein found in the heart, ear, and other tissues. In complex with the KCNE1 accessory protein, it plays a role during the repolarization phase of the cardiac action potential. Mutations in the channel have been associated with several diseases…
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Purification and Membrane Interactions of Human KCNQ1(100–370) Potassium Ion Channel
KCNQ1 (Kv7.1 or KvLQT1) is a voltage-gated potassium ion channel that is involved in the ventricular repolarization following an action potential in the heart. It forms a complex with KCNE1 in the heart and is the pore forming subunit of slow delayed rectifier potassium current (I(ks)). Mutations…
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In vitro-prepared A30P alpha-synuclein fibrils adopt the conserved and disease-relevant Greek key fold
The pathological hallmark of Parkinson Disease (PD) is the formation of the protein alpha-synuclein (Asyn) into β-sheet rich, self-templating fibrils in the brain. Since the first atomic structure of wild-type Asyn fibrils was determined nearly a decade ago, several other in vitro structures of…
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Simple Derivatization of RAFT-Synthesized Styrene–Maleic Anhydride Copolymers for Lipid Disk Formulations
Styrene–maleic acid copolymers have received significant attention because of their ability to interact with lipid bilayers and form styrene–maleic acid copolymer lipid nanoparticles (SMALPs). However, these SMALPs are limited in their chemical diversity, with only phenyl and carboxylic acid…