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Soc."},{"key":"ref30","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/s10822-010-9352-6","article-title":"Ligand docking and binding site analysis with PyMOL and Autodock\/Vina","volume":"24","author":"D Seeliger","year":"2010","journal-title":"J Comput Aided Mol Des"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1002\/pro.5560020312","article-title":"Thioflavine T interaction with synthetic Alzheimer\u2019s disease beta-amyloid peptides: detection of amyloid aggregation in solution","volume":"2","author":"H Levine","year":"1993","journal-title":"Protein Sci"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1006\/abio.1993.1079","article-title":"A self-consistent method for the analysis of protein secondary structure from circular dichroism","volume":"209","author":"N Sreerama","year":"1993","journal-title":"Anal Biochem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/1472-6807-8-25","article-title":"K2D2: Estimation of protein secondary structure from circular dichroism spectra","volume":"8","author":"C Perez-Iratxeta","year":"2008","journal-title":"BMC Struct Biol"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1126\/science.218.4574.747","article-title":"Role of frontier orbitals in chemical reactions","volume":"218","author":"K Fukui","year":"1982","journal-title":"Science"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1289\/ehp.8561191","article-title":"Molecular Electrostatic Potentials: An Effective Tool for the Elucidation of Biochemical Phenomena","volume":"61","author":"P Politzer","year":"1985","journal-title":"Environ Health Perspect"},{"key":"ref36","unstructured":"Hehre WJ, Shusterman AJ, Nelson JE. 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