Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces

PLoS Computational Biology

Volumn 11, Issue 8, 2015, Pages

  Dalgicdir, Cahit ^a   Globisch, Christoph ^b   Peter, Christine ^b   Sayar, Mehmet ^a  

^a KOÇ UNIVERSITY   (Turkey)

^b UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; MOLECULAR DYNAMICS;

ALPHA-HELIX; AMPHIPHILIC PEPTIDES; AMPHIPHILICITY; AMPHIPHILICS; BULK WATER; CONFORMATIONAL PREFERENCES; FOLDINGS; MACROSCOPIC INTERFACES; MOLECULAR INTERFACES; SECONDARY STRUCTURAL ELEMENTS;

PEPTIDES;

GLUTAMYLALANYLALANYLLEUCYLALANYLGLUTAMYLALANYLLEUCYLALANYLGLUTAMYLALANYLLEUCYLALANYLGLUTAMIC ACID; LEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSYLLEUCYLLEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSYLLEUCINE; POLYPEPTIDE; UNCLASSIFIED DRUG; PEPTIDE;

ALPHA HELIX; AMPHIPHILICITY; ARTICLE; CHEMICAL PHENOMENA; COMPLEX FORMATION; CONTROLLED STUDY; ENVIRONMENTAL CHANGE; HYDROPHILICITY; HYDROPHOBICITY; MOLECULAR DYNAMICS; PEPTIDE ANALYSIS; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; ALGORITHM; BIOLOGY; CHEMISTRY; COMPUTER SIMULATION; METABOLISM;

ALGORITHMS; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 84940778612     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1004328     Document Type: Article

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