Structural transitions of porin, a transmembrane protein

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Abstract
Conformational transitions of porin were monitored using 3 independent criteria: (i) oligomeric state as observed by SDS‐polyacrylamide gel electrophoresis; (ii) spectroscopic titrations (ultraviolet and circular dichroism) and (iii) chemical modifications. Four pH‐dependent transitions were observed with half‐maximal changes occurring at pH values of 1.6, 3.5, 11.2 and 12.4. Two of these pH values differ significantly from intrinsic pK values of the constituent amino acids of this membrane protein. Since porin is very polar despite its location predominantly within the outer membranes, this may be due to ion pair formation in the hydrophobic environment of the membrane.