期刊
ANALYTICAL BIOCHEMISTRY
卷 286, 期 1, 页码 1-16出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/abio.2000.4757
关键词
alpha-turn; beta-turn; gamma-turn; delta-turn; pi-turn; sequence-coupled model; 1-4 and 2-3 correlation model; site-independent model; cluster-tolerant capacity
A tight turn in protein structure is defined as a site where (i) a polypeptide chain reverses its overall direction, i.e., leads the chain to fold back on itself by nearly 180 degrees, and (ii) the amino acid residues directly involved in forming the turn. are no more than six. Tight turns are generally categorized as delta -turn, gamma -turn, beta -turn, alpha -turn, and pi -turn, which are formed by two-, three-, four-, five-, and six-amino-acid residues, respectively. According to the folding mode, each of such tight turns can be further classified into several different types. Tight turns play an important role in globular proteins from both the structural and functional points of view. In view of this, various efforts have been made to predict tight turns and their types. This Review summarizes the development in this area, with an emphasis focused on the most recent work concerned that is featured by the sequence-coupled model. Meanwhile, the future challenge in this area has also been briefly addressed. (C) 2000 Academic Press.
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