[NMR paper] NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
Related Articles NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
J Biol Chem. 2017 Mar 09;:
Authors: Sharma AK, Birrane GG, Anklin C, Rigby AC, Alper SL
Abstract
Nitrovasodilators relax vascular smooth muscle cells (VSMC) in part by modulating the interaction of the C-terminal...
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03-11-2017 05:12 PM
[NMR paper] Probing coiled-coil assembly by paramagnetic NMR spectroscopy.
Probing coiled-coil assembly by paramagnetic NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Probing 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...
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[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] 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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11-17-2010 11:15 PM
[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...
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08-22-2010 05:08 PM
The NMR structure of the autophagy-related protein Atg8
The NMR structure of the autophagy-related protein Atg8
Content Type Journal Article
DOI 10.1007/s10858-010-9420-1
Authors
Hiroyuki Kumeta, Hokkaido University Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences Kita 12 Nishi 6 Kita-ku Sapporo 060-0812 Japan
Masahiro Watanabe, Hokkaido University Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences Kita 12 Nishi 6 Kita-ku Sapporo 060-0812 Japan
Hitoshi Nakatogawa, Tokyo Institute of Technology Integrated Research Institute Yokohama 226-8503 Japan
The Autophagy-Related Beclin-1 Protein Requiresthe Coiled-Coil and BARA Domains To Form a Homodimer with SubmicromolarAffinity
Linear Mode
