Circular Dichroism of Collagen and Related Polypeptides
Circular dichroism (CD) spectra are used extensively for studying the conformation of proteins and polypeptides. The correlation of certain spectral features with well-defined peptide conformations has been used to develop computational procedures for conformational analysis (Perczel et al., 1992; Johnson, 1992; Venyaminov et al., 1993). While these procedures yield reasonable estimates of the fractions of a helix, 13 strand and sheet as well as various types of bends present in a test polypeptide, significant fractions are often ascribed “random” or “other” conformations. In these computations, conformations related to structures rich in imino peptide bonds are seldom taken into account. The imino-rich scleroprotein type I collagen and other members of the collagen gene family account for over one-third of the total protein content in the vertebrate body. The conformation of collagen is related to the polyproline II helix. There is growing evidence that many globular proteins may contain small domains with collagenlike structure (Ananthanarayanan et al., 1987; Adzhubei and Sternberg, 1993, 1994). Collagen, polyproline II, and related synthetic polypeptides exhibit CD spectra that appear to be similar to the spectra of many globular proteins in the so-called random coil conformation arising from the collapse of stabilizing interactions.
KeywordsCircular Dichroism Random Coil Globular Protein Triple Helix Positive Band
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