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Frank Delaglio
Researcher at National Institute of Standards and Technology
Publications - 50
Citations - 26351
Frank Delaglio is an academic researcher from National Institute of Standards and Technology. The author has contributed to research in topics: Residual dipolar coupling & Protein structure. The author has an hindex of 29, co-authored 48 publications receiving 25011 citations. Previous affiliations of Frank Delaglio include National Institutes of Health.
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NMRPipe: a multidimensional spectral processing system based on UNIX pipes
TL;DR: The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks.
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Protein backbone angle restraints from searching a database for chemical shift and sequence homology
TL;DR: TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence, and these averages can reliably be used as angular restraints for the protein whose structure is being studied.
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TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts.
TL;DR: Extension of the original 20-protein database to 200 proteins increased the fraction of residues for which backbone angles could be predicted from 65 to 74%, while reducing the error rate from 3 to 2.5%, and addition of a two-layer neural network filter to the database fragment selection process forms the basis for a new program, TALOS+, which further enhances the prediction rate to 88.5%.
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A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Aneta T. Petkova,Yoshitaka Ishii,John J. Balbach,Oleg N. Antzutkin,Richard D. Leapman,Frank Delaglio,Robert Tycko +6 more
TL;DR: A structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1–40) is presented, based on a set of experimental constraints from solid state NMR spectroscopy and incorporates the cross-β structural motif established by x-ray fiber diffraction.
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Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR Spectra
TL;DR: Dipolar couplings obtained from differences in the splittings measured in the oriented and isotropic phases are in excellent agreement with dipolar coupling obtained from direct measurement of the splitting or from a conventional E. COSY-type measurement.