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Distribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins

Overview of attention for article published in PLOS ONE, March 2014
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Title
Distribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins
Published in
PLOS ONE, March 2014
DOI 10.1371/journal.pone.0091129
Pubmed ID
Authors

Liujiao Bian, Xu Ji

Abstract

Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model and parameter to clearly illustrate the feature and characteristic of the unfolding system. Over the past several decades, four approaches have been proposed to describe the interaction between proteins and denaturants, but some ambiguity and deviations usually occur in the explanation of the experimental data.

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The data shown below were compiled from readership statistics for 16 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 16 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 4 25%
Student > Bachelor 3 19%
Professor 2 13%
Student > Master 2 13%
Other 1 6%
Other 1 6%
Unknown 3 19%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 25%
Agricultural and Biological Sciences 3 19%
Pharmacology, Toxicology and Pharmaceutical Science 2 13%
Chemical Engineering 1 6%
Nursing and Health Professions 1 6%
Other 1 6%
Unknown 4 25%