Tsai M.-Y.Yuan J.-M.Yamaki M.CHIH-KAI LINLin S.H.2022-10-122022-10-122013https://www.scopus.com/inward/record.uri?eid=2-s2.0-84885651412&doi=10.1002%2fjccs.201300173&partnerID=40&md5=bd6b0f315311c1ca70c7511e7db287c0https://scholars.lib.ntu.edu.tw/handle/123456789/623486The �?hairpin is a building block in the �?sheet structure. Understanding the formation of the �?hairpin may provide insight into the formation of �?sheet structures in, for example, protein amyloids. In this study, we performed molecular dynamics (MD) simulations to investigate the temperature-dependent transition behaviors of the GB1 �?hairpin peptide. The simulated results are analysed in terms of distances between pairs of peptide bonds and site-dependent dihedral angles. Our results show that the properties of the hairpin can be site-dependent and that the dependency is primarily associated with the hairpin's geometrical shape and specific interactions, such as hydrophobic clustering. Thus our study provides a foundation for the interpretation of probe-dependent experimental results. ? 2013 The Chemical Society Located in Taipei & Wiley-VCH Verlag GmbH & Co. KGaA.Beta-hairpin; MD simulations; Probe-dependent; Protein folding; Site-dependentjournal article10.1002/jccs.2013001732-s2.0-84885651412