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Temperature factor analysis of outer membrane β-stranded porin crystal structures suggests the pore is not uniformly rigid Nature Precedings
S. Krishnaswamy; Abhishek Kumar.
Outer membrane beta-stranded porins form a diverse and complex set of proteins which allow passage of molecules across the membrane interface have been analyzed here from a biophysical and structural perspective using atomic temperature factors or B-factors. Generally atomic temperature factors of molecules from crystal structures indicate the degree of mobility or disorder seen in the crystal structure. Structures of six porins (four 16 stranded beta barrel porins and two 8 stranded beta barrel porins) were taken from the PDB for the analysis based on resolution (better than 3.0 Å) and R-factor (< 0.23). The residue distribution and mobility distribution was found to be characteristic of each of the porins. The mobility and residue...
Tipo: Manuscript Palavras-chave: Biotechnology.
Ano: 2008 URL: http://precedings.nature.com/documents/2495/version/1
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