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Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X.
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Functional estimation of loop-helix boundaries in the lactose permease of Escherichia coli by single amino acid deletion analysis.
Biochemistry. 2001 Feb 20;40(7):1996-2003
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Helices VII and X in the lactose permease of Escherichia coli: proximity and ligand-induced distance changes.
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From membrane to molecule to the third amino acid from the left with a membrane transport protein.
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Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ.
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Site-directed chemical cross-linking demonstrates that helix IV is close to helices VII and XI in the lactose permease.
Biochemistry. 1999 Feb 9;38(6):1715-20
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Tertiary contacts of helix V in the lactose permease determined by site-directed chemical cross-linking in situ.
Biochemistry. 1999 Feb 23;38(8):2320-5
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Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking: helix I is close to helices V and XI.
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Two-dimensional crystallization of Escherichia coli lactose permease.
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Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli.
Biochemistry. 1999 Jun 8;38(23):7407-12
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Proximity relationships between helices I and XI or XII in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking.
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A revised model for the structure and function of the lactose permease. Evidence that a face on transmembrane segment 2 is important for conformational changes.
J Biol Chem. 2000 Jul 28;275(30):23240-6
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Location of helix III in the lactose permease of Escherichia coli as determined by site-directed thiol cross-linking.
Biochemistry. 1999 Dec 21;38(51):16777-82
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Three-dimensional structure of the ion-coupled transport protein NhaA.
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Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: N-ethylmaleimide-sensitive face of helix II.
Biochemistry. 2000 Sep 5;39(35):10649-55
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