AI Article Synopsis
- Large Hydrophobic Residues (LHR) like phenylalanine, isoleucine, leucine, methionine, and valine are crucial for protein structure and function, and this study analyzes their distribution across proteins in 15 different species.
- The research finds that proteins generally maintain around 27% LHR throughout their sequences, with a notable accumulation of these residues in active sites.
- A specific analysis indicates that this 27% frequency of LHR is most pronounced in segments of 45 amino acids, while the influenza virus and P. falciparum show a more random distribution of LHR compared to other organisms.
Article Abstract
Large Hydrophobic Residues (LHR) such as phenylalanine, isoleucine, leucine, methionine and valine play an important role in protein structure and activity. We describe the role of LHR in complete set of protein sequences in 15 different species. That is the distribution of LHR in different proteins of different species is reported. It is observed that the proteins prefer to have 27% of large hydrophobic residues in total and all along the sequence. It is also observed that proteins accumulate more LHR in its active sites. A window analysis on these protein sequences shows that the 27% of LHR is more frequent at window length of 45 amino acids. The influenza virus and P. falciparum show a random distribution of LHR in its proteins compared to other model organisms.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732037 | PMC |
| http://dx.doi.org/10.6026/97320630003409 | DOI Listing |
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