Correction for 'Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis' by Conor M. Haney, et al., Org. Biomol. Chem., 2016, 14, 1584-1592.
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| http://dx.doi.org/10.1039/c6ob90070d | DOI Listing |
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Intracellular pH (pHi) is a crucial parameter in cell biology; thus, a series of pH probes have been developed to determine pHi changes in living cells. However, more sensitive and non-perturbing ratiometric pH probes are needed for accurate pHi measurements. While the fluorescence of circular permutated YFP (cpYFP) is hypersensitive to pH changes due to its intrinsic properties, the single excitation peak of this protein restricts its capacity of becoming a rational type of pH sensor.
View Article and Find Full Text PDFCorrection: Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis.
Org Biomol Chem
June 2016
Department of Chemistry, University of Pennsylvania, 213 South 34th Street, Philadelphia, PA 19104, USA.
Correction for 'Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis' by Conor M. Haney, et al., Org.
View Article and Find Full Text PDFComparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis.
Org Biomol Chem
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Department of Chemistry, University of Pennsylvania, 213 South 34th Street, Philadelphia, PA 19104, USA.
Characterization of the amyloidogenic Parkinson's disease protein α-synuclein (αS) has proven difficult due to its structural plasticity. Here, we present a number of complementary methods to site-specifically introduce fluorescent probes to examine αS fibril formation and cellular uptake. By using various combinations of conventional Cys modification, amber codon suppression, transferase mediated N-terminal modification, and native chemical ligation, several variants of singly- and doubly-labeled αS were produced.
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Boston University School of Medicine, Dept of Physiology and Biophysics, 700 Albany St., Boston, MA 02118, USA. Electronic address:
Background: The molecular details of fatty acid (FA) interactions with albumin are fundamental to understanding transport in the plasma and cellular utilization of these key nutrients and building blocks of membranes.
Scope Of Review: This review focuses on the development and application of NMR methods to study FA binding to albumin [bovine (BSA) and human (HSA)]. The key strategy was to use (13)C enrichment of a specific carbon in the FA as a non-perturbing probe to permit visualization of the small ligand complexed to the very large protein.
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When cell populations are exposed to low-dose alpha-particle radiation, a significant fraction of the cells will not be traversed by a radiation track. However, stressful effects occur in both irradiated and bystander cells in the population. Characterizing these effects, and investigating their underlying mechanism(s), is critical to understanding human health risks associated with exposure to alpha particles.
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