Importance of long-range interactions in (α/β)8 barrel fold |
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Authors: | S Selvaraj and M Michael Gromiha |
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Institution: | (1) Department of Physics, Bharathidasan University, Tiruchirapalli, 620 024 Tamil Nadu, India;(2) RIKEN Life Science Center, 305-0074 Tsukuba, Ibaraki, Japan;(3) Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, 305-0074 Ibaraki, Japan |
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Abstract: | Protein structures are stabilized by both local and long-range interactions. In this work, we analyzed the importance of long-range
interactions in (α/β)8 barrel proteins in terms of residue distances. We found that the residues occurring in the range of 21–30 residues apart
contribute more toward long-range contacts. Indeed, about 50% of successive strands in these proteins are found to occur at
a sequential distance of 21–30 residues. The aromatic amino acid residues Phe, Trp, and Tyr prefer the 4–10 range and all
other residues prefer the 21–30 range. Hydrophobic-hydrophobic resideu pairs are the most preferred ones for long-range interactions
and they may play a key role in the folding and stabilization of (α/β)8 barrel proteins. |
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Keywords: | Long-range contacts secondary structure tertiary structure TIM barrel |
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