Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 23, 2003, Pages 13179-13183

  Angevine, Christine M ^a   Herold, Kelly A G ^a   Fillingame, Robert H ^a  

^a UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SILVER;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; CHEMICAL MODIFICATION; CLUSTER ANALYSIS; CONTROLLED STUDY; CYTOPLASM; MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SURFACE PROPERTY;

ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; BIOLOGICAL TRANSPORT; CELL MEMBRANE; CYSTEINE; CYSTINE; CYTOPLASM; ESCHERICHIA COLI; ETHYLMALEIMIDE; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTON-TRANSLOCATING ATPASES; PROTONS; SILVER; TEMPERATURE; TIME FACTORS;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0345255628     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2234364100     Document Type: Article

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