Authors: Abdur Rahman, Albert Y. Zomaya
Addresses: Advanced Networks Research Group, School of Information Technologies, The University of Sydney, NSW 2006, Australia. ' Advanced Networks Research Group, School of Information Technologies, The University of Sydney, NSW 2006, Australia
Abstract: The importance of protein folding has been recognised for many years. Almost a half century ago, Linus Pauling discovered two quite simple, regular arrangements of amino acids – the α-helix and the β-sheet that are found in almost every protein. In the early 1960s, Christian Anfinsen showed that the proteins actually ||tie|| themselves: If proteins become unfolded, they fold back into proper shape of their own accord; no shaper or folder is needed. The nature of the unfolded state plays a great role in understanding proteins. Alzheimer|s disease, cystic fibrosis, mad cow disease, and many cancers are inherited emphysema. Recent discoveries show that all these apparently unrelated diseases result from protein folding gone wrong. Theoretical and computational studies have recently achieved noticeable success in reproducing various features of the folding mechanism of several small to medium-sized fast-folding proteins. This survey presents the state-of-the-art in protein structure prediction methods from a computer scientist perspective.
Keywords: protein structure prediction; protein folding; algorithms; sequence; tertiary structure; kinetics; folding mechanism; bioinformatics; computational biology.
International Journal of Bioinformatics Research and Applications, 2005 Vol.1 No.1, pp.121 - 143
Available online: 22 Apr 2005 *Full-text access for editors Access for subscribers Purchase this article Comment on this article