Indu R. Chandrashekar

TL;DR: Data show that, while in water and dimethyl sulfoxide, eledoisin prefers to be in an extended chain conformation, whereas in the presence of perdeuterated dodecylphosphocholine micelles, helical conformation is induced in the central core and C-terminal region of the peptide.

TL;DR: The data show that a helical structure is induced in NKB, in presence of perdeuterated dodecyl phosphocholine (DPC) micelles, a membrane model system, which represents a structural motif typical of neurokinin-3 selective agonists.

TL;DR: The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance spectroscopy in both aqueous and membrane mimetic solvents and shows that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core.

TL;DR: The solution structure of NPgamma characterized by circular dichroism (CD) spectropolarimetry and 2D (1)H NMR spectroscopy in both aqueous and membrane mimetic solvents is reported and shows that in water NPGamma prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region of the peptide.

TL;DR: A purely sequence‐dependent approach to the modeling of protein–protein interaction was applied to the study of C‐phycocyanin αβ dimers, which consists of canonical correlation between the hydrophobicity autocorrelation structures of the interacting pairs.