NDLI: Non-random coil behavior as a consequence of extensive PPII structure in the denatured state

Content Provider	PubMed Central
Author	Cortajarena, Aitziber L. Lois, Gregg Sherman, Eilon O’hern, Corey S. Regan, Lynne Haran, Gilad
Abstract	Unfolded proteins may contain native or non-native residual structure, which has important implications for the thermodynamics and kinetics of folding as well as for misfolding and aggregation diseases. However, it has been universally accepted that residual structure should not affect the global size scaling of the denatured chain, which obeys the statistics of random coil polymers. Here we use a single-molecule optical technique, fluorescence correlation spectroscopy, to probe the denatured state of set of repeat proteins containing an increasing number of identical domains, from two to twenty. The availability of this set allows us to obtain the scaling law for the unfolded state of these proteins, which turns out to be unusually compact, strongly deviating from random-coil statistics. The origin of this unexpected behavior is traced to the presence of extensive non-native polyproline II helical structure, which we localize to specific segments of the polypeptide chain. We show that the experimentally observed effects of PPII on the size scaling of the denatured state can be well-described by simple polymer models. Our findings suggest an hitherto unforeseen potential of non-native structure to induce significant compaction of denatured proteins, affecting significantly folding pathways and kinetics.
Related Links	http://dx.doi.org/10.1016/j.jmb.2008.07.005
Ending Page	212
Page Count	10
Starting Page	203
File Format	PDF
ISSN	00222836
e-ISSN	10898638
Journal	Journal of molecular biology
Issue Number	1
Volume Number	382
Language	English
Publisher Date	2008-09-01
Access Restriction	Open
Subject Keyword	Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biophysics

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