Titlebook: Neuropeptide Protocols; G. Brent Irvine,Carvell H. Williams Book 1997 Springer Science+Business Media New York 1997

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The Study of Membrane- or Receptor-Bound Neuropeptides by NMR,mited to uniformly isotope labeled proteins containing 100–150 amino acid residues (.). Owing to overlapping resonances from the receptor, determination of the three-dimensional structure of only the bound ligand may also require uniform isotopic labeling (.N, .C) of the neuropeptide. In light of th

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Book 1997nd a step-by-step set of instructions to enable practitioners to reproduce the method. The Notes section gives insights into pitfalls or critical stages, tips to overcome these obstacles, and sugges­ tions for extensions or modifications of the basic protocol. Neuropeptide Protocols is intended as a

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Purification of Extracted Peptides for Structural Analysis,ovide the protein/peptide chemist with the tools to determine primary structural information on subpicomole quantities of material. This dramatic quantum leap in sequencer sensitivity has made the preparation of samples even more critical with respect to purity. The task of isolating several hundred

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Amino Acid Sequencing of Neuropeptides,ry. This sensitive method is reliable, easy to perform, and the interpretation of the results is straightforward. However, other techniques such as mass spectrometry and enzymatic degradation are needed to confirm the sequence and/or to detect the posttranslational modifications. In this chapter, we