Related ArticlesProbing coiled-coil assembly by paramagnetic NMR spectroscopy.
Org Biomol Chem. 2015 Jan 28;13(4):1159-68
Authors: Zheng T, Boyle A, Robson Marsden H, Valdink D, Martelli G, Raap J, Kros A
Abstract
Here a new method to determine the oligomeric state and orientation of coiled-coil peptide motifs is described. Peptides K and E, which are designed to form a parallel heterodimeric complex in aqueous solution, were labeled with the aromatic amino acids tryptophan and tyrosine on the C-terminus respectively as 'fingerprint' residues. One of the peptides was also labeled with the paramagnetic probe MTSL. One dimensional proton NMR spectroscopy was used to study the peptide quaternary structure by monitoring the signal suppression of the aromatic labels due to proximity of the nitroxyl radical. 1D-NMR confirmed that the peptides K and E form a heterodimeric coiled coil with a parallel orientation. In addition, fluorescence emission quenching of the aromatic labels due to electron exchange with a nitroxyl radical confirmed the parallel coiled coil orientation. Thus, paramagnetic nitroxide and aromatic fluorophore labeling of peptides yields valuable information regarding the quaternary structure from 1D-NMR and steady-state fluorescence measurements. This convenient method is useful not only to investigate coiled coil assembly, but can also be applied to any defined supramolecular assembly.
[NMR paper] NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
Related Articles NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
Protein Pept Lett. 2014 Mar 28;
Authors: Sharma AK, Rigby AC
Abstract
Protein-protein interactions between the C-terminal domain of Myosin Binding Subunit (MBS) of MLC Phosphatase (MBSCT180; C-terminal 180 aa) and the N-terminal coiled coil (CC) leucine zipper (LZ)...
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Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements.
Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements.
Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements.
Protein Sci. 2010 Dec;19(12):2462-74
Authors: Missimer JH, Dolenc J, Steinmetz MO, van Gunsteren WF
Trigger sequences are indispensable elements for coiled-coil formation. The monomeric helical trigger sequence of the yeast transcriptional activator GCN4 has been investigated...
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03-13-2011 04:01 AM
[NMR paper] Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Related Articles Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.
Protein Sci. 2005 Sep;14(9):2421-8
Authors: Schnell JR, Zhou GP, Zweckstetter M, Rigby AC, Chou JJ
Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing...
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12-01-2010 06:56 PM
[NMR paper] NMR solution structure of a highly stable de novo heterodimeric coiled-coil.
NMR solution structure of a highly stable de novo heterodimeric coiled-coil.
Related Articles NMR solution structure of a highly stable de novo heterodimeric coiled-coil.
Biopolymers. 2004 Dec 5;75(5):367-75
Authors: Lindhout DA, Litowski JR, Mercier P, Hodges RS, Sykes BD
The NMR solution structure of a highly stable coiled-coil IAAL-E3/K3 has been solved. The E3/K3 coiled-coil is a 42-residue de novo designed coiled-coil comprising three heptad repeats per subunit, stabilized by hydrophobic contacts within the core and electrostatic...
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11-24-2010 10:03 PM
[NMR paper] Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Related Articles Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe.
Protein Sci. 2001 Aug;10(8):1498-507
Authors: Niccolai N, Spadaccini R, Scarselli M, Bernini A, Crescenzi O, Spiga O, Ciutti A, Di Maro D, Bracci L, Dalvit C, Temussi PA
The design of safe sweeteners is very important for people who are affected by diabetes, hyperlipemia, and caries and other diseases that are linked to the consumption of sugars. Sweet...
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11-19-2010 08:44 PM
[NMR paper] NMR structure of a parallel homotrimeric coiled coil.
NMR structure of a parallel homotrimeric coiled coil.
Related Articles NMR structure of a parallel homotrimeric coiled coil.
Nat Struct Biol. 1998 Aug;5(8):687-91
Authors: Dames SA, Kammerer RA, Wiltscheck R, Engel J, Alexandrescu AT
The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three-stranded, alpha-helical coiled coil, spanning five heptad repeats in the amino acid sequence....
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[NMR paper] Helical and coiled-coil-forming properties of peptides derived from and inhibiting hu
Helical and coiled-coil-forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H-NMR--use of NH temperature coefficients to probe coiled-coil structures.
Related Articles Helical and coiled-coil-forming properties of peptides derived from and inhibiting human immunodeficiency virus type 1 integrase assessed by 1H-NMR--use of NH temperature coefficients to probe coiled-coil structures.
Eur J Biochem. 1998 Apr 1;253(1):236-44
Authors: Krebs D, Maroun RG, Sourgen F, Troalen F, Davoust D,...
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[NMR paper] Heteronuclear NMR assignments and secondary structure of the coiled coil trimerizatio
Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced...
Probing coiled-coil assembly by paramagnetic NMR spectroscopy.
Linear Mode
