Thermodynamics of amyloid dissociation provide insights into aggregate stability regimes

Biophysical Chemistry

Volumn 168-169, Issue , 2012, Pages 10-18

  Brummitt, Rebecca K ^a   Andrews, Jennifer M ^a,c   Jordan, Jacob L ^b,d   Fernandez, Erik J ^b,e   Roberts, Christopher J ^a  

^a UNIVERSITY OF DELAWARE   (United States)

^b University of Virginia   (United States)

^c CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^d GLAXOSMITHKLINE   (United States)

^e BOOZ ALLEN HAMILTON   (United States)

Author keywords

Amyloid dissociation; Amyloid stability; Calorimetry; Protein transfer free energy; Thermodynamic integration

Indexed keywords

AMYLOID; CHYMOTRYPSINOGEN; MONOMER; UREA;

ARTICLE; CALORIMETRY; DISSOCIATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN UNFOLDING; TEMPERATURE; THERMODYNAMICS; THERMOSTABILITY;

AMYLOID; CALORIMETRY; CHYMOTRYPSINOGEN; CIRCULAR DICHROISM; KINETICS; PROTEIN DENATURATION; PROTEIN STABILITY; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 84862994155     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2012.06.001     Document Type: Article

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