Junctophilin-2 (JP2) is a critical structural protein in the heart by stabilizing junctional membrane complexes between the plasma membrane and sarcoplasmic reticula responsible for precise Ca^(2+) regulation. Such complexes are essential for efficient cardiomyocyte contraction and adaptation to altered cardiac workload conditions. Mutations in the JPH2 gene that encodes JP2 are associated with inherited cardiomyopathies and arrhythmias, and disruption of JP2 function is lethal. Interestingly,...
[NMR paper] NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
Non-ribosomal peptide synthetases (NRPSs) are large multienzyme machineries. They synthesize numerous important natural products starting from amino acids. For peptide synthesis functionally specialized NRPS modules interact in a defined manner. Individual modules are either located on a single or on multiple different polypeptide chains. The "peptide-antimicrobial-Xenorhabdus" (PAX) peptide producing NRPS PaxS from Xenorhabdus bacteria...
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[NMR paper] NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.
NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein.
Biomol NMR Assign. 2021 Jan 10;:
Authors: Yanaka S, Yamaguchi Y, Takizawa T, Miyanoiri Y, Yogo R, Shimada I, Kato K
Abstract
The Fc portion of immunoglobulin G (IgG) promotes defensive effector...
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[NMR paper] Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.
Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.
Related Articles Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.
Biomol NMR Assign. 2015 Sep 24;
Authors: Ravotti F, Sborgi L, Cadalbert R, Huber M, Mazur A, Broz P, Hiller S, Meier BH, Böckmann A
Abstract
The apoptosis-associated speck-like protein (ASC protein) plays a central role in eukaryotic innate immune response. Upon infection, multiple ASC molecules assemble into long...
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[NMR paper] 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2
1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
Related Articles 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
J Biomol NMR. 1998 May;11(4):457-8
Authors: Veeraraghavan S, Mello CC, Lee KM, Androphy EJ, Baleja JD
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[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...
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[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...
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[NMR paper] Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from p
Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Related Articles Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Biochemistry. 1991 Jun 4;30(22):5335-40
Authors: Lian LY, Yang JC, Derrick JP, Sutcliffe MJ, Roberts GC, Murphy JP, Goward CR, Atkinson T
Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6988, which retains IgG-binding activity, has been...
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[NMR paper] NMR assignments and secondary structure of the UvrC binding domain of UvrB.
NMR assignments and secondary structure of the UvrC binding domain of UvrB.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR assignments and secondary structure of the UvrC binding domain of UvrB.
FEBS Lett. 1999 May 21;451(2):181-5
Authors: Alexandrovich A, Sanderson MR, Moolenaar GF, Goosen N, Lane AN
The 55 residue C-terminal domain of UvrB that interacts with UvrC during excision repair in Escherichia coli has been expressed and purified as a (His)6 fusion...
NMR resonance assignments of the DNA binding domain of mouse Junctophilin-2
Linear Mode
