Byrne Aimee, Kier Brandon L, Williams D V, Scian Michele, Andersen Niels H
Department of Chemistry, University of Washington Seattle, Washington, 98195, USA
RSC Adv. 2013 Nov 21;2013(43). doi: 10.1039/C3RA43674H.
The Trp-cage, at 20 residues in length, is generally acknowledged as the smallest fully protein-like folding motif. Linking the termini by a two-residue unit and excising one residue affords circularly permuted sequences that adopt the same structure. This represents the first successful circular permutation of any fold of less than 50-residue length. As was observed for the original topology, a hydrophobic staple near the chain termini is required for enhanced fold stability.
由20个残基组成的色氨酸笼通常被认为是最小的完全类似蛋白质的折叠基序。通过一个双残基单元连接末端并切除一个残基可得到采用相同结构的环形排列序列。这代表了长度小于50个残基的任何折叠的首次成功环形排列。正如在原始拓扑结构中所观察到的,链末端附近的疏水钉对于增强折叠稳定性是必需的。