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• W2093674130 abstract "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100Å(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures." @default.
• W2093674130 created "2016-06-24" @default.
• W2093674130 creator A5001441119 @default.
• W2093674130 creator A5030832423 @default.
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• W2093674130 date "2011-02-01" @default.
• W2093674130 modified "2023-09-27" @default.
• W2093674130 title "Non-covalent interactions across subunit interfaces in Sm proteins" @default.
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• W2093674130 doi "https://doi.org/10.1016/j.jtbi.2010.11.025" @default.
• W2093674130 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21095194" @default.
• W2093674130 hasPublicationYear "2011" @default.
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