Search Results - "Alderson, T"
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NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function
Published in Cell (04-02-2021)“…Biomolecules are in constant motion. To understand how they function, and why malfunctions can cause disease, it is necessary to describe their…”
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Unveiling invisible protein states with NMR spectroscopy
Published in Current opinion in structural biology (01-02-2020)“…[Display omitted] •Sparsely populated protein states can play significant biological roles.•NMR spectroscopy can structurally and dynamically characterize…”
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Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Published in Proceedings of the National Academy of Sciences - PNAS (01-05-2018)“…In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and…”
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Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Published in Proceedings of the National Academy of Sciences - PNAS (31-10-2023)“…The AlphaFold Protein Structure Database contains predicted structures for millions of proteins. For the majority of human proteins that contain intrinsically…”
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Local unfolding of the HSP27 monomer regulates chaperone activity
Published in Nature communications (06-03-2019)“…The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here, we describe redox-induced…”
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Automatic structure-based NMR methyl resonance assignment in large proteins
Published in Nature communications (29-10-2019)“…Isotopically labeled methyl groups provide NMR probes in large, otherwise deuterated proteins. However, the resonance assignment constitutes a bottleneck for…”
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A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins
Published in The EMBO journal (15-04-2021)“…HSP27 is a human molecular chaperone that forms large, dynamic oligomers and functions in many aspects of cellular homeostasis. Mutations in HSP27 cause…”
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Activation of caspase-9 on the apoptosome as studied by methyl-TROSY NMR
Published in Proceedings of the National Academy of Sciences - PNAS (19-12-2023)“…Mitochondrial apoptotic signaling cascades lead to the formation of the apoptosome, a 1.1-MDa heptameric protein scaffold that recruits and activates the…”
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Automated assignment of methyl NMR spectra from large proteins
Published in Progress in nuclear magnetic resonance spectroscopy (01-06-2020)“…[Display omitted] •Methyl labeling enables NMR to study large proteins and molecular assemblies.•Assignment of methyl groups is a bottleneck for methyl NMR.•We…”
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Propensity for cis‐Proline Formation in Unfolded Proteins
Published in Chembiochem : a European journal of chemical biology (04-01-2018)“…In unfolded proteins, peptide bonds involving Pro residues exist in equilibrium between the minor cis and major trans conformations. Folded proteins…”
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11
n-dimensional optical orthogonal codes, bounds and optimal constructions
Published in Applicable algebra in engineering, communication and computing (01-11-2019)“…We generalize to higher dimensions the notions of optical orthogonal codes. We establish upper bounds on the capacity of general n -dimensional OOCs, and on…”
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Conditional Disorder in Small Heat-shock Proteins
Published in Journal of molecular biology (17-04-2020)“…Small heat-shock proteins (sHSPs) are molecular chaperones that respond to cellular stresses to combat protein aggregation. HSP27 is a critical human sHSP that…”
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13
Parkinson's disease: Disorder in the court
Published in Nature (London) (04-02-2016)Get full text
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Automatic Assignment of Methyl-NMR Spectra of Supramolecular Machines Using Graph Theory
Published in Journal of the American Chemical Society (19-07-2017)“…Methyl groups are powerful probes for the analysis of structure, dynamics and function of supramolecular assemblies, using both solution- and solid-state NMR…”
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Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy
Published in Journal of magnetic resonance (1997) (01-03-2020)“…[Display omitted] •Changes in hydration radii of small molecules with pressure depend on hydrophobicity.•Diffusion of folded and unfolded proteins can be…”
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PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Published in EMBO reports (04-11-2024)“…Poly(ADP-ribose) polymerase 1 (PARP1) is one of the first responders to DNA damage and plays crucial roles in recruiting DNA repair proteins through its…”
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Disorder in the court
Published in Nature (London) (04-02-2016)“…The native structure of the protein α-synuclein, which is implicated in Parkinson's disease, is controversial. In-cell nuclear magnetic resonance now shows…”
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Tangled web of interactions among proteins involved in iron–sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Published in Biochimica et biophysica acta (01-06-2015)“…Proteins containing iron–sulfur (Fe–S) clusters arose early in evolution and are essential to life. Organisms have evolved machinery consisting of specialized…”
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Monitoring 15 N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Published in Journal of the American Chemical Society (05-07-2018)“…Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. For a two-state folding protein,…”
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Proline isomerization in the C-terminal region of HSP27
Published in Cell stress & chaperones (01-07-2017)“…In mammals, small heat-shock proteins (sHSPs) typically assemble into interconverting, polydisperse oligomers. The dynamic exchange of sHSP oligomers is…”
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