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An expanded view of the protein folding landscape of PDZ domains
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- Hultqvist, Greta, 1980- (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Per Jemth
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- Pedersen, Søren (author)
- University of Copenhagen,Department of Drug Design and Pharmacology
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- Strømgaard, Kristian (author)
- University of Copenhagen,Department of Drug Design and Pharmacology
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- Elsevier BV, 2012
- 2012
- English.
- In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 421:3, s. 550-553
- Journal article (peer-reviewed)
Abstract
Subject headings
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- Most protein domains fold in an apparently co-operative and two-state manner with only the native and denatured states significantly populated at any experimental condition. However, the protein folding energy landscape is often rugged and different transition states may be rate limiting for the folding reaction under different conditions, as seen for the PDZ protein domain family. We have here analyzed the folding kinetics of two PDZ domains and found that a previously undetected third transition state is rate limiting under conditions that stabilize the native state relative to the denatured state. In light of these results, we have re-analyzed previous folding data on PDZ domains and present a unified folding mechanism with three distinct transition states separated by two high-energy intermediates. Our data show that sequence composition tunes the relative stabilities of folding transition states within the PDZ family, while the overall mechanism is determined by topology. This model captures the kinetic folding mechanism of all PDZ domains studied to date.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- PDZ folding transition state
- Biokemi
- Biochemistry
Publication and Content Type
- ref (subject category)
- art (subject category)
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