Structure and Dynamics of Micelle-bound Neuropeptide Y: Comparison with Unligated NPY and Implications for Receptor Selection

NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles

“…In the case of binding interactions, the increased molecular weight of the overall complex will affect the relaxation parameters of each component globally. This effect can be particularly pronounced when a small peptide binds to large micelles (14). In our case, the molecular weight of DPC micelles is roughly 10 times higher than that of mersacidin and lipid II.…”

“…The effect of binding to DPC micelles and lipid II on the mersacidin dynamics are characterized by means of 15 N relaxation together with gradient-edited diffusion experiments. Despite the large number of published solution NMR structural and relaxation dynamics studies of membrane proteins and peptides (12)(13)(14)(15)(16), only a few examples of high resolution NMR studies of protein/peptide-ligand interactions in the presence of membrane-like environments are available to date (17,18). We will show that the differences in sample environments result in substantial conformational changes that modulate the charge accessibility.…”

Receptor Subtype-specific Docking of Asp6.59 with C-terminal Arginine Residues in Y Receptor Ligands

“…However, hydrophobic interactions work only at much shorter range than do ionic interactions, making such scenario not very likely. In a third model, the ligand nonspecifically binds first to the membrane and then enters the receptor (55), probably between TMD5 and 6 (56). The overall size of the binding pocket will then determine how deep the ligand can insert into the receptor.…”

Structurally conserved C-RFa revealed prolactin releasing activity in vitro and gene expression changes in pituitary of seasonally acclimatized carp

“…This characteristic is shared with hPrRP, where it confers more fl exibility to this region. Finally, the common threedimensional arrangement in C-RFa, hPrPR20 and NPY peptide suggest a common and conserved mechanism for receptorrecognition (Bader et al 2001;D'Ursi et al 2002). In the case of C-RFa, the C-terminal amphiphilic alpha-helix could allow interaction with hydrophobic and hydrophilic components of the cell membrane, inducing the bioactive conformation required for receptor binding (D'Ursi et al 2002).…”