Nian E. Zhou
University of Alberta
26 Papers
724 Citations
Nian E. Zhou is an academic researcher from University of Alberta. The author has contributed to research in topics: Protein structure & Hydrophobic effect. The author has an hindex of 21, co-authored 26 publications.
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Papers
Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils.
TL;DR: Analysis of the difference between the ellipticity in benign buffer and in 50% trifluoroethanol and the slope term from a plot of the free energy of unfolding versus guanidine hydrochloride concentration supported the conclusion that the leucine residues at the ends of the coiled-coil are much less buried than in the middle section of thecoil.
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The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils
TL;DR: This study suggests that the folding process for these synthetic model coiled-coils does not involve a single-stranded alpha-helix as a significantly populated folding intermediate and demonstrates that a large number of these weak interactions can play an important role in the assembly of helices.
203
Comparison of antiparallel and parallel two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization.
TL;DR: Urea and guanidine hydrochloride denaturation studies, in conjunction with molecular modeling studies, suggest that there are no physical restrictions to the packing of hydrophobic residues in an antiparallel coiled-coil, however, interchain electrostatic interactions can have positive or negative contributions to the overall stability of the disulfide-bridged coil.
192
Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil.
TL;DR: The results demonstrate that the improvement of protein stability by introduction of a disulfide bond is very relevant to its location and the most effectivedisulfide bonds are those that can be introduced in the hydrophobic core without any disruption of the protein structure.
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Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded alpha-helical coiled-coil.
TL;DR: This de novo designed coiled-coil model protein consists of two identical 35-residue polypeptide chains arranged in a parallel and in-register alignment via interchain hydrophobic interactions and a disulfide bridge at the position 2 between two helices and a single alanine was systematically substituted for a leucine in each chain at position "a" or "d".
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