{"reference": "Chembiochem. 2006 Feb;7(2):257-67", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "entry": "S-0077", "gene_names": "APP, A4, AD1", "remarks": "Aqueous Solution Structure of the Alzheimer's Disease Abeta Peptide (1-42)", "secondary_structure": "DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA#CCSSTTTTTTHHHHHHHHHHHTTTTTTSGGGSSSSTTSSCCC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "16444756", "ligand_smiles": "", "keyword": "Alzheimer's disease amyloid", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA", "uniprot_ac": "P05067", "protein_name": "Amyloid-beta A4 protein", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "1Z0Q", "inchi_key": "", "ec_number": "", "pdb_classification": "PROTEIN BINDING", "type": "Peptide", "author": "Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N.A., Bonvin, A.M., Guerrini, R., Tancredi, T., Temussi, P.A., Picone, D.", "species": "Homo sapiens", "ligand_id": "", "method": "SOLUTION NMR", "ligand_name": "", "global_stoichiometry": "Monomer - A ", "resolution": "", "ligand_formula": "", "length": "42", "ligstr": "", "description": "The conformational path that can lead the ABeta-(1-42) peptide from the native state is experimentally investigated, which is represented by an Alpha helix embedded in the membrane, to the final state in the amyloid fibrils, which is characterized by Beta-sheet structures. The NMR structure solved in HFIP/H2O with high water content showed that, on going from very apolar to polar environments, the long N-terminal helix is essentially retained, whereas the shorter C-terminal helix is lost."}