Reference : Protein dynamics governed by interfaces of high polarity and low packing density.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/16676
Protein dynamics governed by interfaces of high polarity and low packing density.
English
Espinosa Angarica, Vladimir mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) >]
Sancho, Javier [> >]
2012
PloS one
7
10
e48212
Yes (verified by ORBilu)
International
1932-6203
1932-6203
United States
[en] Protein dynamics ; Folding intermediates ; Protein folding
[en] The folding pathway, three-dimensional structure and intrinsic dynamics of proteins are governed by their amino acid sequences. Internal protein surfaces with physicochemical properties appropriate to modulate conformational fluctuations could play important roles in folding and dynamics. We show here that proteins contain buried interfaces of high polarity and low packing density, coined as LIPs: Light Interfaces of high Polarity, whose physicochemical properties make them unstable. The structures of well-characterized equilibrium and kinetic folding intermediates indicate that the LIPs of the corresponding native proteins fold late and are involved in local unfolding events. Importantly, LIPs can be identified using very fast and uncomplicated computational analysis of protein three-dimensional structures, which provides an easy way to delineate the protein segments involved in dynamics. Since LIPs can be retained while the sequences of the interacting segments diverge significantly, proteins could in principle evolve new functional features reusing pre-existing encoded dynamics. Large-scale identification of LIPS may contribute to understanding evolutionary constraints of proteins and the way protein intrinsic dynamics are encoded.
Researchers ; Students
http://hdl.handle.net/10993/16676
10.1371/journal.pone.0048212
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0048212

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