Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm

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

Volumn 110, Issue 11, 2013, Pages 4285-4290

  Moon, C Preston ^a   Zaccai, Nathan R ^a   Fleming, Patrick J ^a   Gessmann, Dennis ^a   Fleming, Karen G ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

Protein folding; Protein sorting; Protein stability

Indexed keywords

ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; OUTER MEMBRANE PHOSPHOLIPASE A; OUTER MEMBRANE PROTEIN W; PHOSPHOLIPASE A; UNCLASSIFIED DRUG;

ARTICLE; CORRELATION ANALYSIS; CYTOPLASM; DENATURATION; ESCHERICHIA COLI; GENE PRODUCT; HYDROPHOBICITY; HYSTERESIS; LIPID BILAYER; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TRANSPORT; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

ACYLTRANSFERASES; BACTERIAL OUTER MEMBRANE PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIPID BILAYERS; MOLECULAR CHAPERONES; PERIPLASM; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 84875037470     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212527110     Document Type: Article

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