蛋白質断片(ペプチド)を用いた蛋白質folding機構解明のNMRによる新しい展開 : turnは果たして高次構造構築に伴う受動的産物か

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This article reviews the findings of recent systematic studies which examine the formation of a secondary structure of protein fragments and their analogue peptides in water solutions through the use of 2D-NMR spectroscopy. Some peptides form a transient secondary structure, and this structure (an elementary twist) then develops into a β-turn or an α-helix, depending upon changes in the environment of the peptide as well as the sequence context. The same formation must also take place in the first step of the folding process of a globular protein, since the formation of an elementary twist is fairly local, depending only on the interaction of a few neighboring residues.
日本生物物理学会の論文