A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima(810 views) Ruggiero A, Dattelbaum JD, Staiano M, Berisio R, D'Auria S, Vitagliano L
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2014 May 15; 9(5): e96560-e96560.
Keywords: Arginine, Binding Protein, Protein Tmargbp, Unclassified Drug, Abc Transporter, Bacterial Protein, Carrier Protein, Ligand, Protein Binding, Amino Acid Sequence, Analytic Method, Article, Binding Site, Carboxy Terminal Sequence, Computer Model, Controlled Study, Dimerization, Molecular Dynamics, Multiwavelength Anomalous Diffraction, Nonhuman, Polyacrylamide Gel Electrophoresis, Protein Conformation, Protein Domain, Protein Interaction, Protein Structure, Simulation, Single Wavelength Anomalous Dispersion, Structure Analysis, Thermotoga Maritima, Calorimetry, Chemistry, Mass Spectrometry, Molecular Genetics, Protein Multimerization, Protein Quaternary Structure, Protein Tertiary Structure, Sequence Homology, Temperature, X Ray Crystallography, Atp-Binding Cassette Transporters, X-Ray, Molecular Sequence Data, Atp-Binding Cassette Transporters Chemistry, Arginine Chemistry, Bacterial Proteins Chemistry, Carrier Proteins Chemistry, Thermotoga Maritima Chemistry,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Napoli, Italy
Department of Chemistry, University of Richmond, Richmond, VA, United States
Laboratory for Molecular Sensing, IBP, CNR, Naples, Italy
References: Not available.
A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima
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