Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding
Document Type
Book Chapter
Publication Date
2010
Keywords
Effect of Counterions, Conformational Stability, Conformational Behavior of Intrinsically Disordered Proteins - Effects of Strong Denaturants, Temperature, PH, Counterions and Macromolecular Crowding
Digital Object Identifier (DOI)
https://doi.org/10.1002/9780470602614.ch19
Abstract
Summary This chapter contains sections titled: Abstract Introduction: Amino Acid Code for Intrinsic Disorder Effects of Strong Denaturants Effect of Temperature Effect of pH Effect of Counterions Effect of Macromolecular Crowding Conclusions Acknowledgments References
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding, in V. N. Uversky & S. Longhi (Eds.), Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation, John Wiley & Sons, p. 545-568
Scholar Commons Citation
Uversky, Vladimir N., "Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding" (2010). Molecular Medicine Faculty Publications. 1076.
https://digitalcommons.usf.edu/mme_facpub/1076
