Both helical propensity and side-chain hydrophobicity at a partially exposed site in alpha-helix contribute to the thermodynamic stability of ubiquitin |
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Authors: | Loladze Vakhtang V Makhatadze George I |
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Institution: | Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, Texas 75390-9038, USA. |
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Abstract: | Pfam family DUF1023 consists entirely of uncharacterized proteins generated by sequencing the genomes of Actinobacteria (Bateman A., et al., Nucleic Acids Res. 2004;32 Database issue:D138-141.) Utilizing sequence similarity detection methods, we infer homology between DUF1023 and alpha/beta hydrolases. DUF1023 proteins conserve the core secondary structures in alpha/beta hydrolase fold, and share similar catalytic machinery as that of alpha/beta hydrolases. We predict DUF1023 spatial structure and deduce that they function as hydrolases utilizing catalytic Ser-His-Asp triad with the serine as a nucleophile. |
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Keywords: | protein stability helical propensity hydrophobicity protein engineering differential scanning calorimetry |
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