Related ArticlesStructures of biomolecular complexes by combination of NMR and cryoEM methods.
Curr Opin Struct Biol. 2017 Jan 02;43:104-113
Authors: Cuniasse P, Tavares P, Orlova EV, Zinn-Justin S
Abstract
CryoEM is presently providing structures of biocomplexes considered intractable to analysis by other structural techniques. NMR is playing an important role in delivering structural information on dynamics events and conformational heterogeneity. Impressive results were obtained by combining cryoEM and either liquid- or solid-state NMR, revealing the structures of cellular machines, filaments and amyloid fibrils. NMR solution structures of proteins and nucleic acids were fitted, together with crystallographic structures, into cryoEM maps of large complexes, to decipher their assembly mechanisms and describe their functional dynamics. Modelling based on solid-state NMR and cryoEM data provided 3D structure of filaments and fibrils. These NMR approaches validated, but also corrected, atomic models built de novo in cryoEM maps, and provided new structural data on flexible or structurally heterogeneous systems. Combination of cryoEM and NMR became an established hybrid approach in structural biology that significantly contributes to our understanding of functional mechanisms in supramolecular assemblies.
PMID: 28056362 [PubMed - as supplied by publisher]
[NMR paper] Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Related Articles Combining NMR and EPR to Determine Structures of Large RNAs and Protein-RNA Complexes in Solution.
Methods Enzymol. 2015;558:279-331
Authors: Duss O, Yulikov M, Allain FH, Jeschke G
Abstract
Although functional significance of large noncoding RNAs and their complexes with proteins is well recognized, structural information for this class of systems is very scarce. Their inherent flexibility causes problems in...
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[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Related Articles Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Publication date: Available online 15 May 2014
Source:Structure</br>
Author(s): Alessandro*A. Rizzo , Margaret*M. Suhanovsky , Matthew*L. Baker , LaTasha*C.R. Fraser , Lisa*M. Jones , Don*L. Rempel , Michael*L. Gross , Wah Chiu , Andrei*T. Alexandrescu , Carolyn*M. Teschke</br>
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique...
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[NMR paper] Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Related Articles Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Curr Opin Biotechnol. 2013 Mar 4;
Authors: Goldbourt A
Abstract
The link of structure and dynamics of biomolecules and their complexes to their function and to many cellular processes has driven the quest for their detailed characterization by a variety of biophysical techniques. Magic-angle spinning solid-state nuclear magnetic resonance spectroscopy...
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[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
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[NMR paper] NMR structures of proteins and protein complexes beyond 20,000 M(r).
NMR structures of proteins and protein complexes beyond 20,000 M(r).
Related Articles NMR structures of proteins and protein complexes beyond 20,000 M(r).
Nat Struct Biol. 1997 Oct;4 Suppl:849-53
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.
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[NMR paper] Computational methods for determining protein structures from NMR data.
Computational methods for determining protein structures from NMR data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Computational methods for determining protein structures from NMR data.
Biochem Pharmacol. 1990 Jul 1;40(1):15-22
Authors: Gippert GP, Yip PF, Wright PE, Case DA
The general procedures by which solution structures of proteins may be deduced from distance and angular constraints derived from NMR are reviewed, with an emphasis on practical aspects of...
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[NMR paper] NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and co
NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Related Articles NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Q Rev Biophys. 1999 Feb;32(1):57-98
Authors: Härd T
Structures of biomolecular complexes by combination of NMR and cryoEM methods.
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