Primary Structure of Major Outer-membrane Protein I (ompF Protein, Porin) of Escherichia Coli B/r

Overview

Journal Biochem J

Specialty Biochemistry

Date 1982 Apr 1

PMID 7049161

Citations 12

Authors

R Chen

C Kramer

W Schmidmayr

U Henning

Affiliations

Soon will be listed here.

Abstract

In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.

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