{"reference": "Biochemistry. 1996 Dec 17;35(50):16094-104", "alternative_name": "", "entry": "S-0053", "gene_names": "", "remarks": "Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment", "secondary_structure": "GSNKGAIIGLM#CCSHHHHHHHC", "chain_id": "", "inchi": "", "amyloid_non_amyloid": "Amyloid", "pmid": "8973180", "ligand_smiles": "", "keyword": "AMYLOID BETA PEPTIDE", "peptide_protein_sequence": "chain-ID A: GSNKGAIIGLM", "uniprot_ac": "P05067", "protein_name": "Amyloid-beta A4 protein", "r_value_free": "", "mutation_s_field": "No", "ligand_mw": "", "pdb_id": "1QCM", "inchi_key": "", "ec_number": "", "pdb_classification": "AMYLOID", "type": "Peptide", "author": "Kohno, T., Kobayashi, K., Maeda, T., Sato, K., Takashima, A.", "species": "Homo sapiens", "ligand_id": "", "method": "SOLUTION NMR", "ligand_name": "", "global_stoichiometry": "", "resolution": "", "ligand_formula": "", "length": "11", "ligstr": "", "description": "The three-dimensional structure of amyloid Beta peptide (25-35), which has neurotoxic activity, in lithium dodecyl sulfate micelles was determined by two-dimensional 1H NMR spectroscopy with simulated annealing calculations. The molecular structure of amyloid Beta peptide in membrane-mimicking environment is composed of a short Alpha helix in the C terminal position. The three residues from the N-terminus are disordered, but the remaining eight C-terminal residues are well-ordered. The four amino acid residues from the N-terminus are hydrophilic and the other seven amino acid residues in C-terminus are hydrophobic. So, our results show that the C-terminal region of amyloid Beta peptide (25-35) is buried in the membrane and assumes Alpha-helical structure, whereas the N-terminal region is exposed to the solvent with a flexible structure. "}