Why Hofmeister effects of many salts favor protein folding but not DNA helix formation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 17, 2010, Pages 7716-7721

  Pegram, Laurel M ^a   Wendorff, Timothy ^a   Erdmann, Robert ^a,b   Shkel, Irina ^a   Bellissimo, Dana ^a   Felitsky, Daniel J ^a,c   Record Jr , M Thomas ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c GLAXOSMITHKLINE   (United States)

Author keywords

Hofmeister salts; m values; Thermodynamics

Indexed keywords

HYDROCARBON; SODIUM CHLORIDE;

ARTICLE; CONTROLLED STUDY; DNA BINDING; DNA DENATURATION; DNA HELIX; PRIORITY JOURNAL; PROTEIN FOLDING; QUANTITATIVE ANALYSIS; THERMODYNAMICS;

CIRCULAR DICHROISM; DNA; HYDROCARBONS; LAC REPRESSORS; MODELS, CHEMICAL; NITROGEN; NUCLEIC ACID CONFORMATION; OXYGEN; PROTEIN FOLDING; SALTS; THERMODYNAMICS;

EID: 77952394693     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913376107     Document Type: Article

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