Interaction with the surrounding water plays a key role in determining the aggregation propensity of proteins

Angewandte Chemie - International Edition

Volumn 53, Issue 15, 2014, Pages 3961-3964

  Chong, Song Ho ^a   Ham, Sihyun ^a  

^a Sookmyung Women's University   (South Korea)

Author keywords

amyloid beta peptides; hydrophobic effect; proteins; thermodynamics; water

Indexed keywords

PEPTIDES; PROTEINS; THERMODYNAMICS; WATER;

AGGREGATION PROPENSITY; AMYLOID BETA-PEPTIDES; EQUILIBRIUM STRUCTURES; HYDRATION FREE ENERGIES; HYDROPHOBIC EFFECT; MOLECULAR DETERMINANTS; PROTEIN HYDROPHOBICITY; PROTEIN-PROTEIN INTERACTIONS;

HYDROPHOBICITY;

AMYLOID BETA PROTEIN; PEPTIDE; WATER;

CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; THERMODYNAMICS;

AMYLOID BETA-PEPTIDES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; PEPTIDES; THERMODYNAMICS; WATER;

EID: 84898078783     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201309317     Document Type: Article

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