Search results for: Jonathan M. Moore

Items from 1 to 11 out of 11 results

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From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins

Aisha Laguerre, Frank Löhr, Erik Henrich, Beate Hoffmann, more

Structure > 2016 > 24 > 10 > 1830-1841

Nanodiscs and isotropic bicelles are promising membrane mimetics in the field of solution nuclear magnetic resonance (NMR) spectroscopy of integral membrane proteins (IMPs). Despite varied challenges to solution NMR studies of IMPs, we attribute the paucity of solution NMR structures in these environments to the inability of diverse IMPs to withstand detergent treatment during standard nanodisc and...

article

Time-shared experiments for efficient assignment of triple-selectively labeled proteins

Frank Löhr, Aisha Laguerre, Christoph Bock, Sina Reckel, more

Journal of Magnetic Resonance > 2014 > 248 > Complete > 81-95

Combinatorial triple-selective labeling facilitates the NMR assignment process for proteins that are subject to signal overlap and insufficient signal-to-noise in standard triple-resonance experiments. Aiming at maximum amino-acid type and sequence-specific information, the method represents a trade-off between the number of selectively labeled samples that have to be prepared and the number of spectra...

article

Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment

Frank Löhr, Sina Reckel, Mikhail Karbyshev, Peter J. Connolly, more

Journal of Biomolecular NMR > 2012 > 52 > 3 > 197-210

Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with ¹⁵N–¹H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce...

article

Crystal Structure of the Ectodomain Complex of the CGRP Receptor, a Class-B GPCR, Reveals the Site of Drug Antagonism

Ernst ter Haar, Christopher M. Koth, Norzehan Abdul-Manan, Lora Swenson, more

Structure > 2010 > 18 > 9 > 1083-1093

Dysregulation of the calcitonin gene-related peptide (CGRP), a potent vasodilator, is directly implicated in the pathogenesis of migraine. CGRP binds to and signals through the CGRP receptor (CGRP-R), a heterodimer containing the calcitonin receptor-like receptor (CLR), a class B GPCR, and RAMP1, a receptor activity-modifying protein. We have solved the crystal structure of the CLR/RAMP1 N-terminal...

article

Refolding and Characterization of a Soluble Ectodomain Complex of the Calcitonin Gene-Related Peptide Receptor

Christopher M. Koth, Norzehan Abdul-Manan, Christopher A. Lepre, Peter J. Connolly, more

Biochemistry > 2010 > 49 > 9 > 1862 - 1872

article

Theory and Applications of NMR-Based Screening in Pharmaceutical Research

Christopher A. Lepre, Jonathan M. Moore, Jeffrey W. Peng

Chemical Reviews > 2004 > 104 > 8 > 3641 - 3676

article

Application of NMR SHAPES Screening to an RNA Target

Eric C. Johnson, Victoria A. Feher, Jeffrey W. Peng, Jonathan M. Moore, more

Journal of the American Chemical Society > 2003 > 125 > 51 > 15724 - 15725

article

The SHAPES strategy: an NMR-based approach for lead generation in drug discovery

Jasna Fejzo, Christopher A Lepre, Jeffrey W Peng, Guy W Bemis, more

Chemistry & Biology > 1999 > 6 > 10 > 755-769

Background: Recently, it has been shown that nuclear magnetic resonance (NMR) may be used to identify ligands that bind to low molecular weight protein drug targets. Recognizing the utility of NMR as a very sensitive method for detecting binding, we have focused on developing alternative approaches that are applicable to larger molecular weight drug targets and do not require isotopic labeling. Results:...

article

NMR screening in drug discovery

Jonathan M Moore

Current Opinion in Biotechnology > 1999 > 10 > 1 > 54-58

NMR methods in drug discovery have traditionally been used to obtain structural information for drug targets or target-ligand complexes. Recently, it has been shown that NMR may be used as an alternative approach for identification of ligands that bind to protein drug targets, shifting the emphasis of many NMR laboratories towards screening and design of potential drug molecules, rather than structural...

article

Microdrop screening: A rapid method to optimize solvent conditions for NMR spectroscopy of proteins

Christopher A. Lepre, Jonathan M. Moore

Journal of Biomolecular NMR > 1998 > 12 > 4 > 493-499

Determining appropriate solvent conditions is a crucial first step for carrying out NMR spectroscopy of proteins, but rapid and efficient methods for doing so are currently lacking. Microdrop screening examines a large number of different solvent conditions using very small amounts of protein and minimal labor. Starting from one initial buffer condition, small aliquots of protein solution are combined...

article

Solution structure of FK506 bound to FKBP-12

Christopher A. Lepre, John A. Thomson, Jonathan M. Moore

FEBS Letters > 1992 > 302 > 1 > 89-96

The complex of the immunosuppressant FK506 bound to FKBP-12 has been studied in solution using ¹ H and inverse-detected ¹ ³ C NMR methods. The resonances of bound, ¹ ³ C-labelled FK506 were assigned and a set of 66 intraligand NOE distance restraints were used to calculate the structure of the bound ligand by distance geometry and restrained molecular dynamics methods...

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