Elucidating the Key Determinants of Structure, Folding, and Stability for the () Conformation of the B1 Domain of Protein G Using Bioinformatics Approaches.

IEEE Transactions on NanoBioscience(2016)

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摘要
The B1 domain of protein G (GB1) is a small, 56 amino acid bacterial immunoglobulin-binding protein with a 4β + α fold. Architecturally, it is composed of a two-layer sandwich consisting of a four-stranded β-sheet that packs against an α-helix. Using several bioinformatics approaches, we investigated which residues may be key determinants of this fold. We identified nine structurally conserved ami...
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关键词
Proteins,Amino acids,Servers,Entropy,Bioinformatics,Three-dimensional displays,Mathematical model
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