Related ArticlesNMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.
J Struct Funct Genomics. 2000;1(1):15-25
Authors: Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA
The solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium thermoautotrophicum has been determined by NMR spectroscopy. MTH1175 is part of a family of conserved hypothetical proteins (COG1433) with unknown functions which contains multiple paralogs from all complete archaeal genomes and the archaeal gene-rich bacterium Thermotoga maritima. Sequence similarity indicates this protein family may be related to the nitrogen fixation proteins NifB and NifX. MTH1175 adopts an alpha/beta topology with a single mixed beta-sheet, and contains two flexible loops and an unstructured C-terminal tail. The fold resembles that of Ribonuclease H and similar proteins, but differs from these in several respects, and is not likely to have a nuclease activity.
Exclusively NOESY-based automated NMR assignment and structure determination of proteins
Exclusively NOESY-based automated NMR assignment and structure determination of proteins
Abstract A fully automated method is presented for determining NMR solution structures of proteins using exclusively NOESY spectra as input, obviating the need to measure any spectra only for obtaining resonance assignments but devoid of structural information. Applied to two small proteins, the approach yielded structures that coincided closely with conventionally determined structures.
Content Type Journal Article
Pages 1-10
DOI 10.1007/s10858-011-9502-8
nmrlearner
Journal club
0
04-01-2011 09:31 PM
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
J Biomol NMR. 2011 Mar 30;
Authors: Ikeya T, Jee JG, Shigemitsu Y, Hamatsu J, Mishima M, Ito Y, Kainosho M, Güntert P
A fully automated method is presented for determining NMR solution structures of proteins using exclusively NOESY spectra as input, obviating the need to measure any spectra only for obtaining resonance assignments but devoid of structural information....
nmrlearner
Journal club
0
03-31-2011 06:24 PM
NMR in a crystallography-based high-throughput protein structure-determination enviro
NMR in a crystallography-based high-throughput protein structure-determination environment.
Related Articles NMR in a crystallography-based high-throughput protein structure-determination environment.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1365-6
Authors: Wüthrich K
An introduction is provided to three papers which compare corresponding protein crystal and NMR solution structures determined by the Joint Center for Structural Genomics (JCSG). Special mention is made of the JCSG strategy for combined use of the two...
nmrlearner
Journal club
0
10-16-2010 03:56 PM
[NMR paper] NMR characterization and solution structure determination of the oxidized cytochrome
NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14396-400
...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] 1H NMR-based determination of the three-dimensional structure of the human plasma fib
1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
Related Articles 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
J Biol Chem. 1993 Apr 25;268(12):8580-9
Authors: Kar L, Lai CS, Wolff CE, Nettesheim D, Sherman S, Johnson ME
Human plasma fibronectin is a plasma glycoprotein that plays an important role in many biological processes. It consists of two...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] 1H NMR-based determination of the secondary structure of porcine pancreatic spasmolyt
1H NMR-based determination of the secondary structure of porcine pancreatic spasmolytic polypeptide: one of a new family of "trefoil" motif containing cell growth factors.
Related Articles 1H NMR-based determination of the secondary structure of porcine pancreatic spasmolytic polypeptide: one of a new family of "trefoil" motif containing cell growth factors.
Biochemistry. 1992 Feb 25;31(7):1998-2004
Authors: Carr MD
Two-dimensional 1H NMR spectroscopy has been used to obtain comprehensive sequence-specific resonance assignments for the...
nmrlearner
Journal club
0
08-21-2010 11:41 PM
PCS-based structure determination of proteinâ??protein complexes
Abstract A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and 1HN/15N chemical shift perturbation is presented. PCS is induced by a paramagnetic lanthanide ion that is attached to a target protein using a lanthanide binding peptide tag anchored at two points. PCS provides long-range (~40 Ã?) distance and angular restraints between the lanthanide ion and the observed nuclei, while the 1HN/15N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure...
nmrlearner
Journal club
0
08-14-2010 04:19 AM
Robust structure-based resonance assignment for functional protein studies by NMR
Abstract High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment...
NMR structure determination and structure-based functional characterization of conser
Linear Mode
