Joseph Agnel Praveen, de Brevern Alexandre G
Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, , Didcot OX11 0QX, UK.
J R Soc Interface. 2014 Apr 16;11(95):20131147. doi: 10.1098/rsif.2013.1147. Print 2014 Jun 6.
Protein folding has been a major area of research for many years. Nonetheless, the mechanisms leading to the formation of an active biological fold are still not fully apprehended. The huge amount of available sequence and structural information provides hints to identify the putative fold for a given sequence. Indeed, protein structures prefer a limited number of local backbone conformations, some being characterized by preferences for certain amino acids. These preferences largely depend on the local structural environment. The prediction of local backbone conformations has become an important factor to correctly identifying the global protein fold. Here, we review the developments in the field of local structure prediction and especially their implication in protein fold recognition.
多年来，蛋白质折叠一直是一个主要的研究领域。尽管如此，导致活性生物折叠形成的机制仍未被完全理解。大量可用的序列和结构信息为识别给定序列的假定折叠提供了线索。实际上，蛋白质结构倾向于有限数量的局部主链构象，其中一些以对某些氨基酸的偏好为特征。这些偏好很大程度上取决于局部结构环境。局部主链构象的预测已成为正确识别全局蛋白质折叠的一个重要因素。在这里，我们综述了局部结构预测领域的进展，特别是它们在蛋白质折叠识别中的意义。
