中程相互作用在蛋白质中的作用。
Role of medium-range interactions in proteins.
作者信息
Ponnuswamy P K, Warme P K, Scheraga H A
出版信息
Proc Natl Acad Sci U S A. 1973 Mar;70(3):830-3. doi: 10.1073/pnas.70.3.830.
Abstract
The energies of oligopeptide segments of lysozyme are minimized with respect to the dihedral angles of the central residue. As the length of the oligopeptide segment increases, up to a nonapeptide, the low-energy conformation becomes that observed in the x-ray structure in most cases. This finding suggests that, while short-range interactions appear to play the dominant role in determining the conformation of an amino-acid residue in a protein, the additional interactions required to stabilize the conformation uniquely may be only of medium range, i.e., those within a nonapeptide, and longer-range interactions may be of considerably less importance.
摘要
溶菌酶的寡肽片段的能量相对于中心残基的二面角被最小化。随着寡肽片段长度增加，直至九肽，在大多数情况下，低能量构象变为在X射线结构中观察到的构象。这一发现表明，虽然短程相互作用似乎在决定蛋白质中氨基酸残基的构象方面起主导作用，但唯一稳定该构象所需的额外相互作用可能仅为中程，即九肽内的那些相互作用，而长程相互作用可能重要性要小得多。
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