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1996, Handbook of biological physics, ISBN 0444824421, Volume 2, 957
In recent years it has become evident that transport processes across membranes play a crucial role in many metabolic systems. The activities of these... 
Biological transport | Biology
eBook
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 02/2017, Volume 114, Issue 7, p. 1530
  Lactose permease (LacY), a paradigm for the largest family of membrane transport proteins, catalyzes the coupled translocation of a galactoside and a H+... 
Proteins | Membranes | E coli | Cytoplasm
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2013, Volume 110, Issue 50, pp. 19984 - 19984
Journal Article
Biophysical Journal, ISSN 0006-3495, 01/2015, Volume 108, Issue 2, p. 28
Journal Article
Biophysical Journal, ISSN 0006-3495, 01/2015, Volume 108, Issue 2, pp. 28a - 28a
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2007, Volume 104, Issue 39, pp. 15294 - 15298
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2014, Volume 111, Issue 5, pp. 1784 - 1788
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2014, Volume 111, Issue 7, pp. 2408 - 2408
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 23, pp. 9361 - 9366
Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated... 
Membrane transport proteins | Proteins | Hydroxyls | Escherichia coli | Atoms | Biochemistry | Sugars | Binding sites | Alkylation | Crystal structure | Membrane protein crystal structure | Bioenergetics | Sugar binding | Affinity labeling | MTS reagents | affinity labeling | MECHANISM | VESICLES | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | membrane protein crystal structure | sugar binding | MODEL | ACTIVE-TRANSPORT | MEMBRANE-TRANSPORT PROTEIN | bioenergetics | SUBSTRATE-BINDING SITE | Galactose - metabolism | Mesylates - metabolism | Substrate Specificity | Cysteine - genetics | Lactose - metabolism | Biological Transport | Membrane Transport Proteins - genetics | X-Ray Diffraction | Escherichia coli - metabolism | Membrane Transport Proteins - metabolism | Cysteine - metabolism | Monosaccharide Transport Proteins - metabolism | Monosaccharide Transport Proteins - genetics | Protein Structure, Tertiary | Crystallization | Models, Molecular | Escherichia coli Proteins - metabolism | Binding Sites - genetics | Cysteine - chemistry | Mesylates - chemistry | Symporters - chemistry | Symporters - metabolism | Membrane Transport Proteins - chemistry | Galactose - chemistry | Escherichia coli - genetics | Symporters - genetics | Escherichia coli Proteins - genetics | Protein Binding | Lactose - chemistry | Protein Conformation | Monosaccharide Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Chemical bonds | Lactose | E coli | Sugar | Index Medicus | MEMBRANE PROTEINS | SACCHAROSE | ESCHERICHIA COLI | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | LACTOSE | CRYSTAL STRUCTURE | 60 APPLIED LIFE SCIENCES | DISULFIDES | INACTIVATION | AFFINITY | COORDINATES | RESIDUES | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2007, Volume 104, Issue 42, pp. 16504 - 16509
According to x-ray structure, the lactose permease (LacY) is a monomer organized into N- and C-terminal six-helix bundles that form a deep internal cavity open... 
Proteins | Molecules | Population growth | Population distributions | Ligands | Biochemistry | Data lines | Sugars | Binding sites | Electrons | Major facilitator superfamily | Double electron-electron resonance | Lactose permease | Membrane transport | Conformational change | CYSTEINE-SCANNING MUTAGENESIS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | CROSS-LINKING | FLANKING HYDROPHILIC DOMAINS | lactose | conformational change | T4 LYSOZYME | permease | SIDE-CHAINS | LINKING IN-SITU | LACTOSE PERMEASE | membrane transport | ELECTRON-ELECTRON RESONANCE | double electron-electron resonance | MEMBRANE-PROTEINS | major facilitator superfamily | Cytoplasm - chemistry | Glycine - genetics | Crystallography, X-Ray | Cysteine - chemistry | Symporters - chemistry | Electron Spin Resonance Spectroscopy - methods | Cysteine - genetics | Glycine - chemistry | Symporters - genetics | Escherichia coli Proteins - genetics | Protein Conformation | Monosaccharide Transport Proteins - chemistry | Mutation | Periplasm - chemistry | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Monosaccharide Transport Proteins - genetics | Lactose | Carrier proteins | Biological transport | Influence | Research | Properties | Membranes | Sugar | Index Medicus | double electron–electron resonance | Biological Sciences | lactose permease
Journal Article