title: Transient non-native helix formation during the folding of β-lactoglobulin.
abstract: In ideal proteins, only native interactions are stabilized step-by-step in a smooth funnel-like energy landscape. In real proteins, however, the transient formation of non-native structures is frequently observed. In this review, the transient formation of non-native structures is described using the non-native helix formation during the folding of β-lactoglobulin as a prominent example. Although β-lactoglobulin is a predominantly β-sheet protein, it has been shown to form non-native helices during the early stage of folding. The location of non-native helices, their stabilization mechanism, and their role in the folding reaction are discussed.
authors: Department of Bioinformatics, Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan. ikeguchi@soka.ac.jp.
authors: Masamichi
authors: M
authors: Ikeguchi
mesh_terms: D000818:Animals; D006801:Humans; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D007782:Lactoglobulins