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5. Genetically probing the regions of ribose-binding protein involved in permease interaction. Eym Y; Park Y; Park C Mol Microbiol; 1996 Aug; 21(4):695-702. PubMed ID: 8878033 [TBL] [Abstract][Full Text] [Related]
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9. Structural prediction of sugar-binding proteins functional in chemotaxis and transport. Argos P; Mahoney WC; Hermodson MA; Hanei M J Biol Chem; 1981 May; 256(9):4357-61. PubMed ID: 6783660 [TBL] [Abstract][Full Text] [Related]
10. The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. Spurlino JC; Lu GY; Quiocho FA J Biol Chem; 1991 Mar; 266(8):5202-19. PubMed ID: 2002054 [TBL] [Abstract][Full Text] [Related]
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12. Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis. Spurlino JC; Rodseth LE; Quiocho FA J Mol Biol; 1992 Jul; 226(1):15-22. PubMed ID: 1619648 [TBL] [Abstract][Full Text] [Related]
13. Stability and folding of precursor and mature tryptophan-substituted ribose binding protein of Escherichia coli. Lee H; Chi SW; Kang M; Baek K; Kim H Arch Biochem Biophys; 1996 Apr; 328(1):78-84. PubMed ID: 8638941 [TBL] [Abstract][Full Text] [Related]
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