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...
[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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[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
Solid-StateNMR Structure Determination from Diagonal-Compensated,Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints
Solid-StateNMR Structure Determination from Diagonal-Compensated,Sparsely Nonuniform-Sampled 4D Proton–Proton Restraints
Rasmus Linser, Benjamin Bardiaux, Loren B. Andreas, Sven G. Hyberts, Vanessa K. Morris, Guido Pintacuda, Margaret Sunde, Ann H. Kwan and Gerhard Wagner
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504603g/aop/images/medium/ja-2014-04603g_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504603g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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07-25-2014 06:55 PM
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
J Comput Biol. 2011 Mar;18(3):347-63
Authors: Jang R, Gao X, Li M
Abstract In NMR resonance assignment, an indispensable step in NMR protein studies, manually processed peaks from both N-labeled and C-labeled spectra are typically used as inputs. However, the use of homologous structures can allow...
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03-10-2011 03:51 PM
Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins
Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 4 January 2011</br>
Jie, Wen , Jihui, Wu , Pei, Zhou</br>
Intrinsically disordered proteins (IDPs) play important roles in many critical cellular processes. Due to their limited chemical shift dispersion, IDPs often require four pairs of resonance connectivities (H?, C?, C? and CO) for establishing sequential backbone assignment. Because most conventional 4-D...
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[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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[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
Linear Mode
