Movements of proteins can be predicted from their amino acid sequence - HealthCanal.com
Movements of proteins can be predicted from their amino acid sequence - HealthCanal.com
Movements of proteins can be predicted from their amino acid sequence HealthCanal.com
Researchers of the VIB department of Structural Biology, in a collaboration within the 'Interuniversity Institute of Bioinformatics in Brussels (IB2)', have developed a method to predict how much the backbone chain of a protein moves based on only its ...
[NMR paper] A suite of amino acid residue type classification pulse sequences for (13)C-detected NMR of proteins.
A suite of amino acid residue type classification pulse sequences for (13)C-detected NMR of proteins.
Related Articles A suite of amino acid residue type classification pulse sequences for (13)C-detected NMR of proteins.
J Magn Reson. 2013 Jul 11;234C:190-196
Authors: Pantoja-Uceda D, Santoro J
Abstract
A suite of (13)C-detected NMR pulse sequences to edit the correlation peaks of the CACO and CON spectra according to the amino acid residue type is presented. The pulse sequences exploit the topology of the C(?) carbon and led to the...
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[NMR paper] Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Chembiochem. 2013 Jan 30;
Authors: Michel E, Skrisovska L, Wüthrich K, Allain FH
Abstract
Current solution NMR techniques enable structural investigations of proteins in molecular particles with sizes...
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02-03-2013 10:19 AM
New amino acid residue type identification experiments valid for protonated and deuterated proteins
New amino acid residue type identification experiments valid for protonated and deuterated proteins
Abstract Two experiments are presented that yield amino acid type identification of individual residues in a protein by editing the 1Hâ??15N correlations into four different 2D subspectra, each corresponding to a different amino acid type class, and that can be applied to deuterated proteins. One experiment provides information on the amino acid type of the residue preceding the detected amide 1Hâ??15N correlation, while the other gives information on the type of its own residue. Versions...
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09-06-2012 05:03 PM
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Abstract Sequence specific resonance assignment constitutes an important step towards high-resolution structure determination of proteins by NMR and is aided by selective identification and assignment of amino acid types. The traditional approach to selective labeling yields only the chemical shifts of the particular amino acid being selected and does not help in establishing a link between adjacent residues along the polypeptide chain, which is important for sequential assignments. An alternative...
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03-20-2012 12:42 AM
[NMR paper] Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments
Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
J Biol Chem. 1996 Mar 22;271(12):6736-45
Authors: Aslund F, Nordstrand K, Berndt KD, Nikkola M, Bergman T, Ponstingl H, Jörnvall H, Otting G, Holmgren A
The primary and...
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[NMR paper] Determinants of protein hyperthermostability: purification and amino acid sequence of
Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Related Articles Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Biochemistry. 1991 Nov 12;30(45):10885-95
Authors: Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard...
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[NMR paper] Determinants of protein hyperthermostability: purification and amino acid sequence of
Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Related Articles Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR.
Biochemistry. 1991 Nov 12;30(45):10885-95
Authors: Blake PR, Park JB, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard...
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08-21-2010 11:12 PM
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D [1H,1H]-NOESY
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D -NOESY
Francesco Fiorito, Torsten Herrmann, Fred F. Damberger and Kurt Wüthrich
Journal of Biomolecular NMR; 2008; 42(1); pp 23-33
Abstract
ASCAN is a new algorithm for automatic sequence-specific NMR assignment of amino acid side-chains in proteins, which uses as input the primary structure of the protein, chemical shift lists of 1HN, 15N, 13Cα, 13Cβ and possibly 1Hα from the previous polypeptide backbone assignment, and one or several 3D 13C- or 15N-resolved -NOESY spectra. ASCAN has also been...
Movements of proteins can be predicted from their amino acid sequence - HealthCanal.com
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