SMoS: a database of structural motifs of protein superfamilies
Shaon Chakrabarti, K. Venkatramanan, Ramanathan Sowdhamini
Abstract
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Shaon Chakrabarti, K. Venkatramanan, Ramanathan Sowdhamini
Abstract
Open-access reader
The Structural Motifs of Superfamilies (SMoS) database provides information about the structural motifs of aligned protein domain superfamilies. Such motifs among structurally aligned multiple members of protein superfamilies are recognized by the conservation of amino acid preference and solvent inaccessibility and are examined for the conservation of other features like secondary structural content, hydrogen bonding, non-polar interaction and residue packing. These motifs, along with their sequence and spatial orientation, represent the conserved core structure of each superfamily and also provide the minimal requirement of sequence and structural information to retain each superfamily fold.
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The Structural Motifs of Superfamilies (SMoS) database provides information about the structural motifs of aligned protein domain superfamilies. Such motifs among structurally aligned multiple members of protein superfamilies are recognized by the conservation of amino acid preference and solvent inaccessibility and are examined for the conservation of other features like secondary structural content, hydrogen bonding, non-polar interaction and residue packing. These motifs, along with their sequence and spatial orientation, represent the conserved core structure of each superfamily and also provide the minimal requirement of sequence and structural information to retain each superfamily fold.
Key concepts: Structural motif, Sequence motif, Computational biology, Structural Classification of Proteins database, Protein structure, Structural alignment, Amino acid residue, Sequence alignment