[NMR paper] AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins
AssignSLP_GUI, a software tool exploiting AI for NMR resonance assignment of sparsely labeled proteins
Not all proteins are amenable to uniform isotopic labeling with ^(13)C and ^(15)N, something needed for the widely used, and largely deductive, triple resonance assignment process. Among them are proteins expressed in mammalian cell culture where native glycosylation can be maintained, and proper formation of disulfide bonds facilitated. Uniform labeling in mammalian cells is prohibitively expensive, but sparse labeling with one or a few isotopically enriched amino acid types is an option...
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11-29-2022 04:03 PM
[NMR paper] Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets
Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets
Sparsely labeled NMR samples provide opportunities to study larger biomolecular assemblies than is traditionally done by NMR. This requires new computational tools that can handle the sparsity and ambiguity in the NMR datasets. The MELD (modeling employing limited data) Bayesian approach was assessed to be the best performing in predicting structures from sparsely labeled NMR data in the 13th edition of the Critical Assessment of Structure Prediction (CASP) event-and limitations of the...
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12-16-2021 10:50 PM
[NMR paper] NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
Related Articles NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.
J Mol Biol. 2019 Apr 26;:
Authors: Chalmers GR, Eletsky A, Morris LC, Yang JY, Tian F, Woods RJ, Moremen KW, Prestegard JH
Abstract
Characterization of proteins using NMR methods begins with assignment of resonances to specific residues. This is usually accomplished using sequential connectivities between nuclear pairs in proteins...
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04-30-2019 03:58 PM
[NMR paper] NMR assignments of sparsely labeled proteins using a genetic algorithm.
NMR assignments of sparsely labeled proteins using a genetic algorithm.
Related Articles NMR assignments of sparsely labeled proteins using a genetic algorithm.
J Biomol NMR. 2017 Mar 13;:
Authors: Gao Q, Chalmers GR, Moremen KW, Prestegard JH
Abstract
Sparse isotopic labeling of proteins for NMR studies using single types of amino acid ((15)N or (13)C enriched) has several advantages. Resolution is enhanced by reducing numbers of resonances for large proteins, and isotopic labeling becomes economically feasible for glycoproteins...
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03-16-2017 06:36 PM
NMR assignments of sparsely labeled proteins using a genetic algorithm
NMR assignments of sparsely labeled proteins using a genetic algorithm
Abstract
Sparse isotopic labeling of proteins for NMR studies using single types of amino acid (15N or 13C enriched) has several advantages. Resolution is enhanced by reducing numbers of resonances for large proteins, and isotopic labeling becomes economically feasible for glycoproteins that must be expressed in mammalian cells. However, without access to the traditional triple resonance strategies that require uniform isotopic labeling, NMR assignment of crosspeaks in...
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03-14-2017 10:36 PM
[NMR paper] Simultaneous assignment and structure determination of protein backbones by using NMR
Simultaneous assignment and structure determination of protein backbones by using NMR dipolar couplings.
Related Articles Simultaneous assignment and structure determination of protein backbones by using NMR dipolar couplings.
Angew Chem Int Ed Engl. 2004 Jun 28;43(26):3479-81
Authors: Jung YS, Sharma M, Zweckstetter M
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11-24-2010 09:51 PM
[NMR paper] Simultaneous assignment and structure determination of a membrane protein from NMR or
Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints.
Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints.
Protein Sci. 2003 Mar;12(3):403-11
Authors: Marassi FM, Opella SJ
A solid-state NMR approach for simultaneous resonance assignment and three-dimensional structure determination of a membrane protein in lipid bilayers is described. The approach is based on the scattering, hence the descriptor "shotgun," of (15)N-labeled amino...
Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets - Frontiers
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