{"method": "SOLUTION NMR", "mutation_s_field": "Yes", "ec_number": "", "description": "The NMR structure of an ABeta17-34 peptide solubilized by the addition of two glutamic acids at each terminus. the ABeta peptide adopts an Alpha-helical structure for residues 19-26 and 28-33. The Alpha-helical structure is broken around residues S26, N27 and K28, which form a kink in the helical conformation. This Alpha-helix was not described earlier in an aqueous solution without organic solvents, and at physiological conditions (pH 7). These data are in agreement with ABeta adopting an Alpha-helical conformation in the membrane before polymerizing into amyloid Beta-sheets and provide insight into the intermediate state of ABeta in Alzheimer's disease. ", "ligstr": "", "pmid": "25284368", "remarks": "Determine the NMR structure of an Abeta 17-34 peptide solubilized by the addition of two glutamic acids at each terminus", "amyloid_non_amyloid": "Amyloid", "type": "Peptide", "inchi": "", "resolution": "", "species": "Homo sapiens", "secondary_structure": "LVFFAEDVGSNKGAIIGL#CCSHHHHTTTHHHHHHHC", "chain_id": "", "gene_names": "", "r_value_free": "", "pdb_id": "2MJ1", "reference": "Biosci Rep. 2014 Nov 24;34(6):e00155.", "keyword": "Amyloid beta A4 protein", "protein_name": "Amyloid-beta A4 protein", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: LVFFAEDVGSNKGAIIGL", "entry": "S-0138", "length": "18", "uniprot_ac": "P05067", "author": "Fonar, G., Samson, A.O.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "", "ligand_name": "", "pdb_classification": "HYDROLASE INHIBITOR", "global_stoichiometry": "", "inchi_key": "", "ligand_id": ""}