Work

Quality Matters: Extension of Clusters of Residues with Good Hydrophobic Contacts Stabilize (Hyper)Thermophilic Proteins

Year: 2014

Type: article

Abstract: Identifying determinant(s) of protein thermostability is key for rational and data-driven protein engineering. By analyzing more than 130 pairs of mesophilic/(hyper)thermophilic proteins, we identified the quality (residue-wise energy) of hydrophobic interactions as a key factor for protein thermostability. This distinguishes our study from previous ones that investigated predominantly structural determinants. Considering this key factor, we successfully discriminated between pairs of mesophilic/(hyper)thermophilic proteins (discrimination accuracy: ∼80%) and searched for structural weak spots in E. coli dihydrofolate reductase (classification accuracy: 70%).

Source: Journal of Chemical Information and Modeling

DOI: 10.1021/ci400568c

Authors: Prakash Chandra Rathi, Hans Wolfgang Höffken, Holger Gohlke

Institutions: Heinrich Heine University Düsseldorf, BASF (Germany)

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

OpenAlex ID: W2015147264

FWCI: 0.991

Cites: 47

Cited by: 12

Related to: 10