Abstract
THE establishment of correlations between solid-state (for example, X-ray) conformations and conformations in solution (monitored by spectroscopic methods such as nuclear magnetic resonance (NMR)) is essential for the understanding of structure–function relationships in biologically active molecules. The relative functional importance of static and dynamic structures is of particular interest for peptide hormones which reach their site(s) of action on the receptor via a fluid medium. We describe here a comparative study of melanostatin (Pro–Leu–Gly–NH2) which acts as a melanocyte stimulating hormone release-inhibiting factor1.
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DESLAURIERS, R., SOMORJAI, R. & RALSTON, E. Correlation between the X-ray structure of melanostatin and its conformation in solution. Nature 266, 746–748 (1977). https://doi.org/10.1038/266746a0
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DOI: https://doi.org/10.1038/266746a0
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