Development of a database of buried polar residues in protein structures

2015 Fiscal Year Final Research Report

• Project/Area Number: 26730148
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Life / Health / Medical informatics
• Research Institution: Tohoku University
• Principal Investigator: Shirota Matsuyuki 東北大学, 医学(系)研究科(研究院), 助教 (00549462)
• Project Period (FY): 2014-04-01 – 2016-03-31
• Keywords: 蛋白質立体構造 / データベース / 水素結合 / 進化的保存

Outline of Final Research Achievements

Although hydrophobic interactions are the driving force of protein folding, polar interactions, such as hydrogen bonds, which buried polar residues make are also important for protein structure and function. However, polar residues that are buried in the protein interior and sequestered from water are considered to be exceptional conformations, whose occurrences, intra-molecular interactions and conservations in natural proteins have not been well studied. In this study, I performed a comprehensive survey of the buried polar residues in the non-redundant protein structures of Protein Data Bank (PDB), focusing on patterns of their side-chain interactions and evolutionary conservation. These results highlight the structural and evolutionary importance of buried polar residues in protein structures and will be beneficial for protein structure prediction and protein design.

Free Research Field

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