Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment

Journal of Physical Chemistry B

Volumn 117, Issue 39, 2013, Pages 11518-11529

  Jang, Hyunbum ^a   Teran Arce, Fernando ^b   Ramachandran, Srinivasan ^b   Kagan, Bruce L ^c   Lal, Ratnesh ^b   Nussinov, Ruth ^a,d  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; GLYCOPROTEINS; LIPID BILAYERS; MOLECULAR DYNAMICS; NEURODEGENERATIVE DISEASES; PEPTIDES;

ALZHEIMER'S DISEASE; AMYLOID PRECURSOR PROTEINS; CHANNEL TOPOLOGY; CONFORMATIONAL PREFERENCES; CONFORMATIONAL STATE; DELETION MUTANTS; MOLECULAR DYNAMICS SIMULATIONS; NEGATIVELY CHARGED;

CONFORMATIONS;

1,2 OLEOYLPHOSPHATIDYLCHOLINE; 1,2-OLEOYLPHOSPHATIDYLCHOLINE; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); AMYLOID PRECURSOR PROTEIN; APP PROTEIN, HUMAN; PEPTIDE FRAGMENT; PHOSPHATIDYLCHOLINE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; GENE DELETION; GENETICS; HUMAN; LIPID BILAYER; MOLECULAR DYNAMICS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PEPTIDES; AMYLOID BETA-PROTEIN PRECURSOR; BINDING SITES; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIPID BILAYERS; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PHOSPHATIDYLCHOLINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE DELETION;

EID: 84885138277     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp405389n     Document Type: Article

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