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Article
Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction
A single experimental method alone often fails to provide the resolution, accuracy, and coverage needed to model integral membrane proteins (IMPs). Integrating computation with experimental data is a powerful ...
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Article
Open AccessStructural details of a Class B GPCR-arrestin complex revealed by genetically encoded crosslinkers in living cells
Understanding the molecular basis of arrestin-mediated regulation of GPCRs is critical for deciphering signaling mechanisms and designing functional selectivity. However, structural studies of GPCR-arrestin co...
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Article
Determination of G-protein–coupled receptor oligomerization by molecular brightness analyses in single cells
Oligomerization of membrane proteins has received intense research interest because of their importance in cellular signaling and the large pharmacological and clinical potential this offers. Fluorescence imag...
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Article
Allosteric interactions in the parathyroid hormone GPCR–arrestin complex formation
Peptide ligands of class B G-protein-coupled receptors act via a two-step binding process, but the essential mechanisms that link their extracellular binding to intracellular receptor–arrestin interactions are...
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Protocol
Map** of Protein Interfaces in Live Cells Using Genetically Encoded Crosslinkers
Understanding the topology of protein-protein interactions is a matter of fundamental importance in the biomedical field. Biophysical approaches such as X-ray crystallography and nuclear magnetic resonance can...
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Article
Erratum: Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity
Nat. Methods 10, 885–888 (2013); published online 4 August 2013; corrected after print 21 November 2013 In the version of this article initially published, in Figure 2e, lanes 6 and 8 should have been labeled ...
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Article
Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity
An unnatural amino acid that forms a covalent bond with a proximal cysteine can be introduced into proteins, facilitating a variety of applications.
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Chapter and Conference Paper
The depsipeptide technique for the solid phase peptide synthesis: from stepwise assembly to segment condensation
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Article
Solid-phase peptide synthesis: from standard procedures to the synthesis of difficult sequences
This protocol for solid-phase peptide synthesis (SPPS) is based on the widely used Fmoc/tBu strategy, activation of the carboxyl groups by aminium-derived coupling reagents and use of PEG-modified polystyrene ...
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Chapter and Conference Paper
N,O-Acyl Shifts: Unexpected Side-Reaction and Beneficial Tool in Fmoc-Chemistry
