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Volumn 135, Issue 20, 2011, Pages

Amyloid-β peptide structure in aqueous solution varies with fragment size

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL FREE ENERGY; FRAGMENT SIZES; N-TERMINALS; PEPTIDE STRUCTURES; POTENTIAL OF MEAN FORCE; REPLICA-EXCHANGE MOLECULAR DYNAMICS SIMULATIONS; SALT BRIDGES; SECONDARY AND TERTIARY STRUCTURES; SECONDARY STRUCTURES; SHEET STRUCTURE; THERMODYNAMIC CALCULATIONS;

EID: 82555173714     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3662490     Document Type: Article
Times cited : (47)

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    • See supplementary material at E-JCPSA6-135-007144 for intra-molecular interactions using different distance criteria. This document also contains the average secondary structure abundances of each peptide, the radius of gyration probability distributions of each peptide, PMF convergence test results, -helix and -sheet content associated with their G, secondary structure abundances of each PMF basin for each peptide, intra-molecular interactions for the structures located in each PMF basin for each peptide, and formed salt bridges for the structures located in each PMF basin for each peptide
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