Porins are integral membrane proteins found in the outer membrane of bacteria, mitochondria and
chloroplasts. Herein, we have reviewed sequence and structural understanding about bacterial porins. The
first porin structure from Rhodobacter capsulatus at 1.8 Å resolution in 1991 till the recent structural advancement,
coupled by immunological properties, diffusion and ion permeation has been taken into account
In the later part, we have presented our computational analysis of conformational mobility in selected
porins. Atomic B-factors (in crystal structures) are indicative of the degree of intrinsic mobility associated
with residues and secondary structural elements of a particular protein. We have explored and extended the
intrinsic motilities within porins using selected six porins structures. These six porins were collected from
PDB and B-factor analyses were performed using AWK scripts. Distributions of residues and mobilities were characteristic
of different porins. These distribution patterns follow the level of homology at the sequence and structural level. The
inner walls constituting the trimer interface were found to be more rigid than the outer walls. These mobility differences
are intrinsic structural components of these porins.
Keywords: B-factor (atomic temperature factor), β-stranded porins, conformational mobility, membrane proteins, porins.
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