Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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51167 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set |
Chemical Shift Assignment of Methionine-Oxidized Alpha-Synuclein Bound to SDS Micelles | On the effect of methionine oxidation on the interplay between alpha-synuclein and synaptic-like vesicles | Ana Belen Uceda Mayo, Bartolome Vilanova Canet, Juan Frau Munar, Miquel Adrover Estelrich |
50896 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set |
Chemical Shift Assignment of SDS micelle-bound alpha-synuclein homogeneusly modified with CEL | Glycation of alpha-synuclein hampers its binding to synaptic-like vesicles and its driving effect on their fusion | Ana Belen Uceda, Bartolome Vilanova, Juan Frau, Miquel Adrover |
50895 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set |
Chemical Shift Assignment of Human Alpha-Synuclein bound to SDS micelles | Glycation of alpha-synuclein hampers its binding to synaptic-like vesicles and its driving effect on their fusion | Ana Belen Uceda, Bartolome Vilanova, Juan Frau, Miquel Adrover |
27796 | Chemical Shifts: 1 set |
Chemical Shift Assignments for native alpha-synuclein | Unravelling the effect of N(epsilon)-(carboxyethyl)lysine on the conformation, dynamics and aggregation propensity of alpha-synuclein | Bartolome Vilanova, Joaquin Ortega-Castro, Juan Frau, Laura Marino, Miquel Adrover, Rafael Ramis, Rodrigo Casasnovas |
27797 | Chemical Shifts: 1 set |
Chemical Shift Assignments for alpha-synuclein homogeneously modified with CEL | Unravelling the effect of N(epsilon)-(carboxyethyl)lysine on the conformation, dynamics and aggregation propensity of alpha-synuclein | Bartolome Vilanova, Joaquin Ortega-Castro, Juan Frau, Laura Marino, Miquel Adrover, Rafael Ramis, Rodrigo Casasnovas |
25524 | Chemical Shifts: 1 set |
NMR structure of Neuromedin C in 90% TFE | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, Juan Jesus Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25525 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
NMR structure of Neuromedin C in presence of SDS micelles | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, J Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25523 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
NMR structure of Neuromedin C in 60% TFE | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, Juan Jesus Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25519 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
NMR structure of Neuromedin C in aqueous solution. | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, J Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25520 | Chemical Shifts: 1 set |
NMR structure of Neuromedin C in 10% TFE | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, Juan Jesus Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25521 | Chemical Shifts: 1 set |
NMR structure of Neuromedin C in 25% TFE | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, J Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
25522 | Chemical Shifts: 1 set |
NMR structure of Neuromedin C in 40% TFE | Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism | Bartolome Vilanova, Gabriel Martorell, J Perez, Kris Pauwels, Miquel Adrover, Pilar Sanchis |
17641 | Chemical Shifts: 1 set |
Assigment of the 1H, 13C, and 15N resonances of the yeast frataxin (Yfh1) under heat denaturation (50 C) | The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. | Annalisa Pastore, Dmitri I Svergun, Dunja Urosev, Gabriel Martorell, Miquel Adrover, Petr V Konarev, Pierandrea Temussi, Stephen R Martin, Xavier Daura |
17068 | Chemical Shifts: 1 set |
Assigment of the 1H, 13C, and 15N resonances of the yeast frataxin (Yfh1) under cold denaturation | Understanding cold denaturation: the case study of yfh1. | Annalisa Pastore, Gabriel Martorell, Miquel Adrover, Piero Andrea Temussi, Veronica Esposito |
16706 | Chemical Shifts: 1 set |
1H, 13C, and 15N chemical shift assignments for H2H2, a mini prion protein | Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3. | Annalisa Pastore, Celine Chapuis, Cesira de Chiara, Human Rezaei, Kris Pauwels, Miquel Adrover, Stephanie Prigent, Zhou Xu |