CONFORMATIONAL ANALYSIS OF A CHAIN REVERSAL IN α-CHYMOTRYPSIN
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 8 (6) , 543-550
- https://doi.org/10.1111/j.1399-3011.1976.tb02534.x
Abstract
A complete conformational analysis of the fold (Asp-Lys-Thr-Gly) (residues 35-38), and additional adjacent residues of .alpha.-chymotrypsin was performed. A comparison of these findings with those of Lewis et al. is made, and a discussion of the implications of protein-fold models is discussed. This particular residue sequence prefers to bend over maintaining a helical conformation. However, the bend conformation of the tetramer is different from that of the native bend. The native bend conformation is nearly realized when an additional residue of the native primary structure is added to each side of the tetramer. Early and late folding-sequence studies suggests that while the native fold is of low energy, there are fold-points along the primary structure which are more stable. The structural implications of this finding are discussed.This publication has 13 references indexed in Scilit:
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