On Unsatisfied Hydrogen Bonds in the N-Terminal Subdomain of Villin Headpiece
نویسندگان
چکیده
منابع مشابه
A thermostable 35-residue subdomain within villin headpiece.
The actin-bundling protein villin contains, at its extreme C terminus, a compact f-actin binding domain called "headpiece". This 76-amino acid domain from chicken is highly thermostable. Here, we show that the stable folded structure in headpiece is localized to a subdomain formed by the C-terminal 35 residues. The subdomain, denoted HP-35, is monomeric and retains high thermostability, with a ...
متن کاملEffect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain.
Equilibrium Fourier transform infrared (FTIR) and temperature-jump (T-jump) IR spectroscopic techniques were used to study the thermodynamics and kinetics of the unfolding and folding of the villin headpiece helical subdomain (HP36), a small three-helix protein. A double phenylalanine mutant (HP36 F47L, F51L) that destabilizes the hydrophobic core of this protein also was studied. The double mu...
متن کاملDynamic folding pathway models of the villin headpiece subdomain (HP-36) structure
We have investigated the folding pathway of the 36-residue villin headpiece subdomain (HP-36) by action-derived molecular dynamics simulations. The folding is initiated by hydrophobic collapse, after which the concurrent formation of full tertiary structure and alpha-helical secondary structure is observed. The collapse is observed to be associated with a couple of specific native contacts cont...
متن کاملAn unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain.
A reversible structural unlocking reaction, in which the close-packed van der Waals interactions break cooperatively, has been found for the villin headpiece subdomain (HP35) using triplet-triplet-energy transfer to monitor conformational fluctuations from equilibrium. Unlocking is associated with an unfavorable enthalpy change (DeltaH(0) = 35 +/- 4 kJ/mol) which is nearly compensated in free e...
متن کاملQuantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments.
As the fastest folding protein, the villin headpiece (HP35) serves as an important bridge between simulation and experimental studies of protein folding. Despite the simplicity of this system, experiments continue to reveal a number of surprises, including structure in the unfolded state and complex equilibrium dynamics near the native state. Using 2.5 ms of molecular dynamics and Markov state ...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2011
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2011.08.024