Morphology and persistence length of amyloid fibrils are correlated to peptide molecular structure

Journal of the American Chemical Society

Volumn 133, Issue 45, 2011, Pages 18030-18033

  Vandenakker, Corianne C ^a   Engel, Maarten F M ^a   Velikov, Krassimir P ^b,c   Bonn, Mischa ^a,d   Koenderink, Gijsje H ^a  

^a FOM INSTITUTE AMOLF   (Netherlands)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

^c UTRECHT UNIVERSITY   (Netherlands)

^d MAX PLANCK INSTITUTE FOR POLYMER RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID STRUCTURES; AMYLOID-RELATED DISEASE; ASSEMBLY PROCESS; GROWTH CONDITIONS; LACTOGLOBULIN; MOLECULAR CONFORMATION; PERSISTENCE LENGTH; SELF ASSEMBLY PROCESS; VIBRATIONAL SUM-FREQUENCY GENERATIONS;

ASSEMBLY; ATOMIC FORCE MICROSCOPY; ATOMIC SPECTROSCOPY; MECHANICAL PROPERTIES; MOLECULAR STRUCTURE; MORPHOLOGY; PEPTIDES;

GLYCOPROTEINS;

AMYLOID; BETA LACTOGLOBULIN; PEPTIDE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CHEMICAL STRUCTURE; CONFORMATION; PROTEIN POLYMORPHISM; SPECTROSCOPY;

AMYLOID; PEPTIDES; PROTEIN CONFORMATION;

EID: 80755129361     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja206513r     Document Type: Article

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