Literature DB >> 19122773

A HAUSDORFF-BASED NOE ASSIGNMENT ALGORITHM USING PROTEIN BACKBONE DETERMINED FROM RESIDUAL DIPOLAR COUPLINGS AND ROTAMER PATTERNS.

Jianyang Michael Zeng1, Chittaranjan Tripathy, Pei Zhou, Bruce R Donald.   

Abstract

High-throughput structure determination based on solution Nuclear Magnetic Resonance (NMR) spectroscopy plays an important role in structural genomics. One of the main bottlenecks in NMR structure determination is the interpretation of NMR data to obtain a sufficient number of accurate distance restraints by assigning nuclear Overhauser effect (NOE) spectral peaks to pairs of protons. The difficulty in automated NOE assignment mainly lies in the ambiguities arising both from the resonance degeneracy of chemical shifts and from the uncertainty due to experimental errors in NOE peak positions. In this paper we present a novel NOE assignment algorithm, called HAusdorff-based NOE Assignment (HANA), that starts with a high-resolution protein backbone computed using only two residual dipolar couplings (RDCs) per residue37, 39, employs a Hausdorff-based pattern matching technique to deduce similarity between experimental and back-computed NOE spectra for each rotamer from a statistically diverse library, and drives the selection of optimal position-specific rotamers for filtering ambiguous NOE assignments. Our algorithm runs in time O(tn(3) +tn log t), where t is the maximum number of rotamers per residue and n is the size of the protein. Application of our algorithm on biological NMR data for three proteins, namely, human ubiquitin, the zinc finger domain of the human DNA Y-polymerase Eta (pol η) and the human Set2-Rpb1 interacting domain (hSRI) demonstrates that our algorithm overcomes spectral noise to achieve more than 90% assignment accuracy. Additionally, the final structures calculated using our automated NOE assignments have backbone RMSD < 1.7 Å and all-heavy-atom RMSD < 2.5 Å from reference structures that were determined either by X-ray crystallography or traditional NMR approaches. These results show that our NOE assignment algorithm can be successfully applied to protein NMR spectra to obtain high-quality structures.

Entities:  

Year:  2008        PMID: 19122773      PMCID: PMC2613371     

Source DB:  PubMed          Journal:  Comput Syst Bioinformatics Conf        ISSN: 1752-7791


  29 in total

Review 1.  Automated analysis of NMR assignments and structures for proteins.

Authors:  H N Moseley; G T Montelione
Journal:  Curr Opin Struct Biol       Date:  1999-10       Impact factor: 6.809

2.  The penultimate rotamer library.

Authors:  S C Lovell; J M Word; J S Richardson; D C Richardson
Journal:  Proteins       Date:  2000-08-15

3.  Cyclic coordinate descent: A robotics algorithm for protein loop closure.

Authors:  Adrian A Canutescu; Roland L Dunbrack
Journal:  Protein Sci       Date:  2003-05       Impact factor: 6.725

4.  Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.

Authors:  Torsten Herrmann; Peter Güntert; Kurt Wüthrich
Journal:  J Mol Biol       Date:  2002-05-24       Impact factor: 5.469

5.  The Xplor-NIH NMR molecular structure determination package.

Authors:  Charles D Schwieters; John J Kuszewski; Nico Tjandra; G Marius Clore
Journal:  J Magn Reson       Date:  2003-01       Impact factor: 2.229

6.  Automated NMR structure calculation with CYANA.

Authors:  Peter Güntert
Journal:  Methods Mol Biol       Date:  2004

7.  Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.

Authors:  Ming Li; Hemali P Phatnani; Ziqiang Guan; Harvey Sage; Arno L Greenleaf; Pei Zhou
Journal:  Proc Natl Acad Sci U S A       Date:  2005-11-28       Impact factor: 11.205

8.  Inferential structure determination.

Authors:  Wolfgang Rieping; Michael Habeck; Michael Nilges
Journal:  Science       Date:  2005-07-08       Impact factor: 47.728

9.  Automated combined assignment of NOESY spectra and three-dimensional protein structure determination.

Authors:  C Mumenthaler; P Güntert; W Braun; K Wüthrich
Journal:  J Biomol NMR       Date:  1997-12       Impact factor: 2.835

10.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology.

Authors:  G Cornilescu; F Delaglio; A Bax
Journal:  J Biomol NMR       Date:  1999-03       Impact factor: 2.835

View more
  4 in total

1.  NVR-BIP: Nuclear Vector Replacement using Binary Integer Programming for NMR Structure-Based Assignments.

Authors:  Mehmet Serkan Apaydin; Bülent Çatay; Nicholas Patrick; Bruce R Donald
Journal:  Comput J       Date:  2011-05-01       Impact factor: 1.494

2.  Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.

Authors:  Bruce R Donald; Jeffrey Martin
Journal:  Prog Nucl Magn Reson Spectrosc       Date:  2009-08-01       Impact factor: 9.795

3.  High-resolution protein structure determination starting with a global fold calculated from exact solutions to the RDC equations.

Authors:  Jianyang Zeng; Jeffrey Boyles; Chittaranjan Tripathy; Lincong Wang; Anthony Yan; Pei Zhou; Bruce Randall Donald
Journal:  J Biomol NMR       Date:  2009-08-27       Impact factor: 2.835

4.  Experimental Protein Structure Verification by Scoring with a Single, Unassigned NMR Spectrum.

Authors:  Joseph M Courtney; Qing Ye; Anna E Nesbitt; Ming Tang; Marcus D Tuttle; Eric D Watt; Kristin M Nuzzio; Lindsay J Sperling; Gemma Comellas; Joseph R Peterson; James H Morrissey; Chad M Rienstra
Journal:  Structure       Date:  2015-09-10       Impact factor: 5.006

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.