Youtao Song, Manli Shen

School of Environment

Linan Xu , Jianwei He

School of Life Sciences

Abstract

The protein folding problem (PFP), which is still considered to be one of the most daunting challenges for scientists, is the question of how a protein’ s amino acid sequence dictates its three-dimensional protein structure. The notion of a folding “problem” first emerged around 1960, with the appearance of the first atomic-resolution protein structures. The major milestones in PFP solving were Anfinsen’ s thermodynamic hypothesis and Levinthal paradox, which made in the late of 1960s and early of 1970s. During the last 40 years, besides the traditional molecular biological techniques, many new theoretical and computational approaches have arisen, such as multiple-sequence alignments, molecular dynamics simulations, and the Critical Assessment of Techniques for Protein Structure Prediction (CASP) community-wide event for protein structure prediction. Current computer algorithms are now predicting native structures of small proteins with remarkable accuracy. Especially, for the once seemingly intractable Levinthal puzzle, there is a viable hypothesis now: A protein can fold quickly and solve its big global optimization puzzle by piecewise solutions of smaller component puzzles.

Read the article here:     113-Roles of hydrophobic and hydrophilic forces on maintaining amyloid-prone cystatin structural stability.pdf