Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Abstract One bottleneck in NMR structure determination lies in the laborious and time-consuming process of side-chain resonance and NOE assignments. Compared to the well-studied backbone resonance assignment problem, automated side-chain resonance and NOE assignments are relatively less explored. Most NOE assignment algorithms require nearly complete side-chain resonance assignments from a series of through-bond experiments such as HCCH-TOCSY or HCCCONH. Unfortunately, these TOCSY...
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06-27-2011 04:30 AM
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
[NMR paper] Resonance assignment of proteins with high shift degeneracy based on 5D spectral info
Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments.
Related Articles Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments.
J Am Chem Soc. 2005 Apr 6;127(13):4554-5
Authors: Atreya HS, Eletsky A, Szyperski T
A suite of novel (5,3)D G2FT triple resonance NMR experiments encoding highly resolved 5D spectral information is presented for sequential resonance assignment of proteins exhibiting high chemical...
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11-25-2010 08:21 PM
[NMR paper] A modified strategy for sequence specific assignment of protein NMR spectra based on
A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
Related Articles A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
J Biomol NMR. 2005 Feb;31(2):115-28
Authors: Schubert M, Labudde D, Leitner D, Oschkinat H, Schmieder P
The determination of the three-dimensional structure of a protein or the study of protein-ligand interactions requires the assignment of all relevant nuclei as an initial step....
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11-24-2010 11:14 PM
[NMR paper] Histogram-based scoring schemes for protein NMR resonance assignment.
Histogram-based scoring schemes for protein NMR resonance assignment.
Related Articles Histogram-based scoring schemes for protein NMR resonance assignment.
J Bioinform Comput Biol. 2004 Dec;2(4):747-64
Authors: Wan X, Tegos T, Lin G
In NMR protein structure determination, after the resonance peaks have been identified and chemical shifts from peaks across multiple spectra have been grouped into spin systems, associating these spin systems to their host residues is the key toward the success of structural information extraction and thus the...
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11-24-2010 10:03 PM
[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
Related Articles NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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11-24-2010 08:49 PM
13C-direct detected NMR experiments for the sequential J-based resonance assignment o
Abstract We present here a set of 13C-direct detected NMR experiments to facilitate the resonance assignment of RNA oligonucleotides. Three experiments have been developed: (1) the (H)CC-TOCSY-experiment utilizing a virtual decoupling scheme to assign the intraresidual ribose 13C-spins, (2) the (H)CPC-experiment that correlates each phosphorus with the C4â?² nuclei of adjacent nucleotides via J(C,P) couplings and (3) the (H)CPC-CCH-TOCSY-experiment that correlates the phosphorus nuclei with the respective C1â?²,H1â?² ribose signals. The experiments were applied to two RNA hairpin structures....
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08-14-2010 04:19 AM
Robust structure-based resonance assignment for functional protein studies by NMR
Abstract High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment...
GFT NMR based resonance assignment for the 21 kDa human protein UFC1.
Linear Mode
