Detecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping
Detecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping
Abstract
Peak lists derived from nuclear magnetic resonance (NMR) spectra are commonly used as input data for a variety of computer assisted and automated analyses. These include automated protein resonance assignment and protein structure calculation software tools. Prior to these analyses, peak lists must be aligned to each other and sets of related peaks must be grouped based on common chemical shift dimensions. Even when...
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[NMR paper] Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
FEBS Lett. 2014 Aug 25;588(17):2851-8
Authors: Cho HY, Ul Mushtaq A, Lee JY, Kim DG, Seok MS, Jang M, Han BW, Kim S, Jeon YH
Abstract
Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor...
[NMR paper] (1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
(1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles (1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
Biomol NMR Assign. 2013 Apr;7(1):1-4
Authors: Nogaret S, Guittet E, Birlirakis N
Abstract
CGC-19, a 14 kDa proteic constituent of a non...
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08-30-2013 04:35 PM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
[NMR paper] Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepar
Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis.
Related Articles Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis.
J Am Chem Soc. 2004 Mar 3;126(8):2439-46
Authors: Kochendoerfer GG, Jones DH, Lee S, Oblatt-Montal M, Opella SJ, Montal M
Vpu is an 81-residue integral membrane protein encoded in the HIV-1 genome that is of considerable interest because it plays important roles in the release of virus particles...
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11-24-2010 09:25 PM
[NMR paper] Dissecting functional interactions in coagulation protein complexes by use of NMR spe
Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Related Articles Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Curr Protein Pept Sci. 2002 Jun;3(3):275-85
Authors: Tolkatchev D, Koutychenko A, Ni F
The blood coagulation cascade can be considered as a system of well-orchestrated protein activation reactions involving and leading to the formation of large macromolecular assemblies. NMR investigations performed during the last six years have focused...
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11-24-2010 08:49 PM
[NMR paper] Structural characterization of peptide hormone/receptor interactions by NMR spectrosc
Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
Biopolymers. 1999;51(3):208-20
Authors: Pellegrini M, Mierke DF
The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled...