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

Prakash Chandra Rathi | Zendy; Hans Wolfgang Höffken | Zendy; Holger Gohlke | Zendy

Open Access

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

Author(s) -

Prakash Chandra Rathi,

Hans Wolfgang Höffken,

Holger Gohlke

Publication year - 2014

Publication title -

journal of chemical information and modeling

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.24

H-Index - 160

eISSN - 1549-960X

pISSN - 1549-9596

DOI - 10.1021/ci400568c

Subject(s) - thermostability , thermophile , mesophile , chemistry , protein engineering , computational biology , protein structure , residue (chemistry) , hydrophobic effect , protein folding , biochemistry , biology , enzyme , genetics , bacteria

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%).

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