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Inter-residue interactions play an important role in governing the folding and stability of protein structures. In this work, we have analyzed the contacts between amino acid residues in different folding types of globular proteins and various ranges of folding rates. Based on amino acid contacts a novel parameter, multiple contact index has been developed for understanding protein folding rates....
Usually prediction of molecular functions of proteins from their amino acid sequences is based upon sequence similarity with proteins of known functions. However, it is well known that function is mainly dependent upon protein structures than sequences. Since structures are often independent of sequences, it is important to predict function without sequence similarities. Here we propose a method based...
We have utilized neural networks in different applications of bioinformatics such as discrimination of beta-barrel membrane proteins, mesophilic and thermophilic proteins, different folding types of globular proteins, different classes of transporter proteins and predicting the secondary structures of beta-barrel membrane proteins. In these methods, we have used the information about amino acid composition,...
Cation-π interactions play an important role to the stability of protein structures. In this work, we analyze the influence of cation-π interactions in three-dimensional structures of membrane proteins. We found that transmembrane strand (TMS) proteins have more number of cation-π interactions than transmembrane helical (TMH) proteins. In TMH proteins, both the positively charged residues Lys and...
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