Structure Determination of Micelle-Bound NPY

In our experience resonance assignment is speeded up so much in the case of 15N-la-beled peptides that the additional effort in the laboratory is quickly paid for. The HSQC spectra will also help to immediately recognize signal overlap. 

The three-dimensional structure of NPY when bound to the membrane is shown in Fig. 5.6. It comprises an a-helix for residues 16 to 36 which is very well defined, and a flexible N-terminal part of the molecule. When comparing the structure of the DPC-mi-celle bound form to the structure in free solution, it is obvious that the a-helix is much more stable. In addition, the C-terminus of the helix comprising residues 32-36, which is flexible in solution, adopts an a-helical fold, and the Tyr36 is oriented such that it interacts with the water-membrane interface. 

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