Physical interaction between the phage lambda receptor protein and the carrier-immobilized maltose-binding protein of Escherichia coli.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
1. Cellular Transport Mechanisms
2. Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein.
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1. Tuning the Affinity of Anion Binding Sites in Porin Channels with Negatively Charged Residues: Molecular Details for OprP;ACS Chemical Biology;2014-10-31
2. Maltose Binding Protein (MBP);Encyclopedia of Molecular Biology;2002-01-15
3. Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein;Journal of Molecular Biology;1992-02
4. Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane;Journal of Biological Chemistry;1991-01
5. Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein;Journal of Molecular Biology;1990-07
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