Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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[NMR paper] A modified strategy for sequence specific assignment of protein NMR spectra based on
A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
Related Articles A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
J Biomol NMR. 2005 Feb;31(2):115-28
Authors: Schubert M, Labudde D, Leitner D, Oschkinat H, Schmieder P
The determination of the three-dimensional structure of a protein or the study of protein-ligand interactions requires the assignment of all relevant nuclei as an initial step....
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[NMR paper] Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific ass
Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure.
Eur J Biochem. 1994 Jun 15;222(3):1047-54
Authors: Petit MC, Sodano P, Marion D, Ptak M
Correlation spectroscopy (COSY), total correlation...
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[NMR paper] Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific ass
Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure.
Eur J Biochem. 1994 Jun 15;222(3):1047-54
Authors: Petit MC, Sodano P, Marion D, Ptak M
Correlation spectroscopy (COSY), total correlation...
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[NMR paper] A relational database for sequence-specific protein NMR data.
A relational database for sequence-specific protein NMR data.
Related Articles A relational database for sequence-specific protein NMR data.
J Biomol NMR. 1991 Sep;1(3):217-36
Authors: Seavey BR, Farr EA, Westler WM, Markley JL
A protein NMR database has been designed and is being implemented. The database is intended to contain solution NMR results from proteins and peptides (larger than 12 residues). A relational database format has been chosen that indexes data by: primary journal citation, molecular species, sequence-related and...
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08-21-2010 11:12 PM
[NMR paper] A relational database for sequence-specific protein NMR data.
A relational database for sequence-specific protein NMR data.
Related Articles A relational database for sequence-specific protein NMR data.
J Biomol NMR. 1991 Sep;1(3):217-36
Authors: Seavey BR, Farr EA, Westler WM, Markley JL
A protein NMR database has been designed and is being implemented. The database is intended to contain solution NMR results from proteins and peptides (larger than 12 residues). A relational database format has been chosen that indexes data by: primary journal citation, molecular species, sequence-related and...
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Sequence specific resonance assignment via Multicanonical Monte Carlo search using an ABACUS approach
Sequence specific resonance assignment via Multicanonical Monte Carlo search using an ABACUS approach
Alexander Lemak, Carlos A. Steren, Cheryl H. Arrowsmith and Miguel Llinás
Journal of Biomolecular NMR; 2008; 41(1); pp 29 - 41
Abstract:
ABACUS is a novel protocol for automated protein structure determination via NMR. ABACUS starts from molecular fragments defined by unassigned J-coupled spin-systems and involves a Monte Carlo stochastic search in assignment space, probabilistic sequence selection, and assembly of fragments into structures that are used to guide the stochastic...
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08-14-2008 12:37 AM
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH
Jochen Volk, Torsten Herrmann and Kurt Wüthrich
Journal of Biomolecular NMR; 2008; 41(3); pp 127 - 138
Abstract:
MATCH (Memetic Algorithm and Combinatorial Optimization Heuristics) is a new memetic algorithm for automated sequence-specific polypeptide backbone NMR assignment of proteins. MATCH employs local optimization for tracing partial sequence-specific assignments within a global, population-based search environment, where the simultaneous application of local and global optimization heuristics...
Influence of Quasi-Specific Sites on Kinetics of TargetDNA Search by a Sequence-Specific DNA-Binding Protein
Linear Mode
