Joel Lapin
College of Sciences
Works (6)
Updated: July 7th, 2023 21:13
2022 article
Validation of protein backbone structures calculated from NMR angular restraints using Rosetta (vol 73, pg 229, 2019)
Lapin, J., & Nevzorov, A. A. (2022, August 27). JOURNAL OF BIOMOLECULAR NMR.
TL;DR:
A framework for de-novo protein structure prediction using a combination of solid-state NMR angular restraints and bioinformatics is established and Rosetta was able to distinguish the most plausible structures.
(via Semantic Scholar)
open access via link.springer.com (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: September 12, 2022
2020 journal article
Computer-generated pulse sequences for H-1-N-15 and H-1(alpha)-C-13(alpha) separated local-field experiments
JOURNAL OF MAGNETIC RESONANCE, 317.
author keywords: NMR pulse sequence design; Automation; Simulated annealing; GPU computing; Separated local field experiments; Dipolar couplings; PISEMA; SAMPI4; ROULETTE
TL;DR:
The new algorithm, in addition to finding pulse durations and phases, now searches for the optimal on/off application scheme of radio frequency irradiation on each channel, effectively optimizing every aspect of a pulse sequence instead of just phases and durations.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 24, 2020
2020 journal article
H-1/C-13/N-15 triple-resonance experiments for structure determinaton of membrane proteins by oriented-sample NMR
SOLID STATE NUCLEAR MAGNETIC RESONANCE, 111.
author keywords: NMR pulse sequence design; Triple-resonance experiments; Dipolar couplings; Separated local-field spectroscopy; ROULETTE; Membrane proteins; Structure determination; Heteronuclear correlations
MeSH headings : Magnetic Resonance Imaging; Magnetic Resonance Spectroscopy / methods; Membrane Proteins / chemistry; Nuclear Magnetic Resonance, Biomolecular / methods; Protons
TL;DR:
The presented developments advance NMR of oriented samples for structure determination of membrane proteins and liquid crystals in solid-state NMR experiments.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: March 8, 2021
2019 journal article
De novo NMR pulse sequence design using Monte-Carlo optimization techniques
JOURNAL OF MAGNETIC RESONANCE, 310.
MeSH headings : Algorithms; Bacteriophage Pf1 / chemistry; Capsid Proteins / chemistry; Computer Simulation; Crystallization; Hydrogen; Leucine / analogs & derivatives; Leucine / chemistry; Monte Carlo Method; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular / methods
TL;DR:
A computational strategy was developed to find the optimal phases and timings that substantially improve the 1H-15N dipolar linewidths over a broad range of dipolar couplings as compared to SAMPI4.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: January 13, 2020
2019 journal article
NMR "Crystallography" for Uniformly (C-13, N-15)-Labeled Oriented Membrane Proteins
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 59(9), 3554–3557.
author keywords: dipolar couplings; membrane proteins; nuclear magnetic resonance; oriented samples; structure determination
MeSH headings : Carbon Isotopes / chemistry; Inovirus / metabolism; Isotope Labeling; Lipid Bilayers / chemistry; Lipid Bilayers / metabolism; Membrane Proteins / chemistry; Nitrogen Isotopes / chemistry; Nuclear Magnetic Resonance, Biomolecular; Viral Proteins / chemistry
TL;DR:
A new experimental triple-resonance NMR technique was applied to uniformly doubly labeled Pf1 coat protein in magnetically aligned DMPC/DHPC bicelles and yielded a consensus α-helical transmembrane structure for Pf1 protein.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: February 10, 2020
2019 journal article
Validation of protein backbone structures calculated from NMR angular restraints using Rosetta
JOURNAL OF BIOMOLECULAR NMR, 73(5), 229–244.
author keywords: Oriented-sample NMR; Angular restraints; Dipolar couplings; Chemical shift anisotropy; Membrane proteins; Structure determination; Rosetta
MeSH headings : Magnetic Resonance Spectroscopy / methods; Membrane Proteins / chemistry; Protein Conformation
TL;DR:
A significantly improved version of the algorithm which includes the fitting of several peptide planes at once in order to prevent propagation of error along the backbone and establishes a framework for de-novo protein structure prediction using a combination of solid-state NMR angular restraints and bioinformatics.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: July 1, 2019
Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.
Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.