A Deterministic Approach to the Protein Design Problem
Maksim Skorobogatiy, Hong Guo, Martin J. Zuckermann
Abstract
We have considered the problem of protein design based on a model where the contact energy between amino acid residues is fitted phenomenologically using the Miyazawa--Jernigan matrix. Due to the simple form of the contact energy function, an analytical prescription is found which allows us to design energetically stable sequences for fixed amino acid residues compositions and target structures. The theoretically obtained sequences are compared with real proteins and good correspondence is obtained. Finally we discuss the effect of discrepancies in the procedure used to fit the contact energy on our theoretical predictions.
Create a lesson
Related papers
Potential energy release rate for solids with bounded domains during evolutions involving changes to boundaries and boundary data
Mrityunjay Kothari, Sayaka Kochiyama, Haneesh Kesari
Arrested phase separation and amorphous patterns in charged binary fluids
Logan H. Grant, Ana Bensabat, Eva Pospivsilova et al.
Shear-driven arrest of dip-coating film entrainment
Theo Witkamp, Stéphane Zaleski, Federico Toschi
How Fluctuations Control Chiral Symmetry Breaking in Reacting Mixtures of Chiral Molecules
Leonardo Silva-Dias, Christoph A. Weber
A new device for live cell imaging of biological samples under in-plane shear
Sidharth Kumar Das, Lyova Mamoyan, Eberhard Bodenschatz et al.
Imbibition dynamics under dissolution-driven fluid thickening
H. W. Almeida, A. F. V. Matias, R. C. V. Coelho et al.