• Publications
  • Influence
Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
  • C. Moon, K. Fleming
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences
  • 23 May 2011
The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. MeasurementsExpand
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Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A.
Ubiquitin-associated (UBA) domains are small protein domains that occur in the context of larger proteins and are likely to function as inter- and intramolecular communication elements inExpand
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β-Barrel Proteins That Reside in the Escherichia coli Outer Membrane in Vivo Demonstrate Varied Folding Behavior in Vitro*
Little is known about the dynamic process of membrane protein folding, and few models exist to explore it. In this study we doubled the number of Escherichia coli outer membrane proteins (OMPs) forExpand
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Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA
Significance The folding of outer membrane proteins (OMPs) in biological membranes in vivo requires an evolutionarily conserved and essential protein, β-barrel assembly machinery subunit A (BamA). ByExpand
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Specificity in transmembrane helix–helix interactions can define a hierarchy of stability for sequence variants
  • K. Fleming, D. Engelman
  • Medicine, Chemistry
  • Proceedings of the National Academy of Sciences…
  • 27 November 2001
The folding, stability, and oligomerization of helical membrane proteins depend in part on a precise set of packing interactions between transmembrane helices. To understand the energetic principlesExpand
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Standardizing the free energy change of transmembrane helix-helix interactions.
  • K. Fleming
  • Medicine, Chemistry
  • Journal of molecular biology
  • 25 October 2002
Side-to-side associations of transmembrane alpha-helices are integral components of the structure and function of helical membrane proteins. A fundamental unknown in the understanding of the chemicalExpand
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Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm
Thermodynamic stabilities are pivotal for understanding structure–function relationships of proteins, and yet such determinations are rare for membrane proteins. Moreover, the few measurements thatExpand
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What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
Here we describe how the systematic redesign of a protein's hydrophobic core alters its structure and stability. We have repacked the hydrophobic core of the four‐helix‐bundle protein, Rop, withExpand
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Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer.
To quantify the relationship between sequence and transmembrane dimer stability, a systematic mutagenesis and thermodynamic study of the protein-protein interaction residues in the glycophorin AExpand
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Computation and mutagenesis suggest a right‐handed structure for the synaptobrevin transmembrane dimer
Biological membrane fusion involves a highly precise and ordered set of protein–protein interactions. Synaptobrevin is a key player in this process. Mutagenesis studies of its single transmembraneExpand
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