Guide for Studies on Structure and Function Employing Synthetic Polypeptides
The systematic design of protein tertiary structure poses a formidable challenge in protein engineering. Several years ago we undertook the design of models for those peptides and proteins for which to a first approximation tertiary structure can be neglected (Kroon et al., 1978; Kaiser and Kezdy, 1983, 1984). Although the prediction of tertiary structure from primary sequence cannot as yet be made with confidence, it was our thesis that secondary structures could be built in a rational fashion. Furthermore, the reasonable hypothesis was proposed that in amphiphilic environments like that of a biological interface, complementary amphiphilic secondary structures (secondary structures having distinct hydrophobic and hydro- philic faces) may be induced in peptides and proteins binding on such interfaces. Therefore, as our initial objective we engaged in the modeling of peptides and proteins that have affinity for membranes.
KeywordsPeptide Hormone Salmon Calcitonin Model Peptide Helix Axis Human Calcitonin
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