Marx DC, Leblanc MJ, Plummer AM, Krueger S, Fleming KG. (2020) Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA. Protein Sci. doi: 10.1002/pro.3924. PMID: 32748422
O'Brien ES, Fuglestad B, Lessen HJ, Stetz MA, Lin DW, Marques BS, Gupta K, Fleming KG, Wand AJ.(2020) Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angew Chem Int Ed Engl. 26;59(27):11108-11114. doi: 10.1002/anie.202003527. PMID: 32277554
Alford RF, Fleming PJ, Fleming KG, Gray JJ. (2020) Protein Structure Prediction and Design in a Biologically Realistic Implicit Membrane. Biophys J. Apr 21;118(8):2042-2055. doi: 10.1016/j.bpj.2020.03.006. PMID: 32224301
Lessen HJ, Majumdar A, Fleming KG. (2020) Backbone Hydrogen Bond Energies in Membrane Proteins Are Insensitive to Large Changes in Local Water Concentration. J Am Chem Soc. Apr 1;142(13):6227-6235. doi: 10.1021/jacs.0c00290. PMID: 32134659
Chum AP, Shoemaker SR, Fleming PJ, Fleming KG. (2019) Plasticity and transient binding are key ingredients of the periplasmic chaperone network. Protein Sci. 28(7):1340-1349. PMID: 31074917
Lessen HJ, Fleming PJ, Fleming KG, Sodt AJ. (2018) Building Blocks of the Outer Membrane: Calculating a General Elastic Energy Model for β-Barrel Membrane Proteins. J Chem Theory, 14(8):4487-4497. PMID:29979594
Fleming PJ & KG Fleming (2018) Hullrad: “Fast Calculations of Folded and Disordered Protein and Nucleic Acid Hydrodynamic Properties” Biophys J114: 856-869. PMID: 29490246.
KG Fleming(2018) “Taking Deterministic Control of Membrane Protein Monomer-dimer Measurements” J Gen Physiol 150: 181-183. PMID: 29343502.
Peterson JH, Plummer AM, Fleming KG& HD Bernstein (2017) “Selective Pressure for Rapid Membrane Integration Constrains the Sequence of Bacterial Outer Membrane Proteins” Mol Microbiol.106: 777-792. PMID: 28941249
Marx DC & KG Fleming (2017) “Influence of Protein Scaffold on Side-Chain Transfer Free Energies”Biophys J113: 597-604.PMID: 28793214
Mo GC, Ross B, Hertel F, Manna P, Yang X, Greenwald E, Booth C, Plummer AM, Tenner B, Chen Z, Wang Y, Kennedy EJ, Cole PA, Fleming KG, Palmer A, Jimenez R, Xiao J, Dedecker P & J Zhang (2017) “Genetically Encoded Biosensors for Visualizing Live-Cell Biochemical Activity at Super-resolution” Nat Methods 14: 427-434. PMID: 28288122
Danoff EJ and KG Fleming (2017) “Novel kinetic intermediates along the folding pathway of OmpA” Biochemistry 10;56(1):47-60. doi: 10.1021/acs.biochem.6b00809. Epub 2016 Dec 21.
McDonald SK and KG Fleming (2016) “Negative charge neutralization in the loops and turns of outer membrane phospholipase A impacts folding hysteresis at neutral pH” Biochemistry 55: 6133-6137. PMID: 27731977 DOI: 10.1021/acs.biochem.6b00652; PMCID: In Progress.
Costello SM, Plummer AM, Fleming PJ & KG Fleming (2016) “Dynamic Periplasmic Chaperone Reservoir Facilitates Biogenesis of Outer Membrane Proteins” PNAS 113: E4794-800. PMID: 27482090; PMCID: PMC4995976.
Plummer AM and KG Fleming (2016) “From Chaperones to the Membrane with a BAM!” Trends Biochem. Sci. 41:872-882. This article was highlighted on the cover of the October 2016 issue. PMID: 27450425; PMCID: PMC In Progress; DOI: 10.1016/j.tibs.2016.06.005.
McDonald SK and KG Fleming (2016) “Aromatic Side Chain Water-to-Lipid Transfer Free Energies Show a Depth-Dependence Across the Membrane Normal” J. Am Chem. Soc. 138: 7946-50. PMID: 27254476; PMCID: 4927395; DOI: 10.1021/jacs.6b03460.
Fleming PJ, Patel DS, Wu EL, Qi Y, Yeom MS, Sousa MC, Fleming KG and W Im (2016) “BamA POTRA Domain Interacts with a Native Lipid Membrane Surface” Biophys. J. 110: 2698-2709. PMID: 27332128; PMCID: PMC4919588 DOI: 10.1016/j.bpj.2016.05.010.
McDonald SK and KG Fleming (2016) “Aromatic Side Chain Water-to-Lipid Transfer Free Energies Show a Depth-Dependence Across the Membrane Normal” Am Chem. Soc. In Press. PMID: 27254476; PMCID: In Process.
Zaccai NR, Sandlin CW, Hoopes JT, Curtis JE, Fleming PJ, Fleming KG and S Krueger (2016) “Deuterium labeling together with contrast variation small-angle neutron scattering suggests how Skp captures and releases unfolded outer membrane proteins” (2015) Methods Enzymol 566 159-210. PMID: 26791979; PMCID: In Process.
Sandlin CW, Zaccai NR and KG Fleming (2015) “Skp trimer formation is insensitive to ionic strength” Biochemistry 54: 7059-7062. PMID: 26579730; PMCID: In Process.
Plummer AM and KG Fleming (2015) “BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism” Biochemistry 54: 6009-6011. PMID: 26394056; PMCID: PMC4613867.
Danoff EJ and KG Fleming (2015) “Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils Upon Self-Association” PLos ONE 10: e0132301. PMID: 26196893; PMCID: PMC4509890
Fleming KG (2015) “A kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria” Phil Trans R Soc Lond B Biol Sci 370: PMID: 26370938;
Danoff EJ and KG Fleming (2015) “Membrane defects accelerate outer membrane b-barrel protein folding” Biochem 54: 97-99. PMID: 25513891; PMCID: PMC4303321.
Wu EL, Fleming PJ, Yeom MS, Widmalm G, Klauda JB, Fleming KG and W Im (2014) “E coli Outer Membrane and Interactions with OmpLA” J. 106: 2493. PMID: 24896129; PMCID: PMC4052237.
Gessmann D, Chung YH, Danoff EJ, Plummer AM, Sandlin CW, Zaccai NR and KG Fleming (2014) “Outer membrane b-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA” PNAS 111: 5878-93. PMID: 24715731; PMCID: PMC4000854.
Fleming KG (2014) “Energetics of Membrane Protein Folding” Ann Rev Biophys 43: 233-55. PMID: 24895854; PMCID Pending.
Moon CP, Zaccai NR, Fleming PJ, Gessmann D and KG Fleming (2013) “Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm” PNAS 110: 4285-4290. PMID: 23440211; PMCID: PMC3600475.
Buchanan SK, Yamashita Y and KG Fleming (2012) “Structure and folding of outer membrane proteins” in Comprehensive Biophysics EH Egelman and LK Tamm, Oxford: Academic Press Vol 5: 139-163.
Moon CP, Kwon S and KG Fleming (2011) “Overcoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers” J. Biol. 413: 484-494. PMID: 21888919; PMCID: PMC3193555.
Fleming PJ, Freites JA, Moon CP, Tobias DJ and KG Fleming (2011) “Outer membrane phospholipase A in phospholipid bilayers: A model system for concerted computational and experimental investigations of amino acid side chain partitioning into lipid bilayers” BBA Biomembranes 1818: 126-134. PMID: 21816133; PMCID: PMC3233656.
Danoff EJ and KG Fleming (2011) “The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane b-barrel” Chem. 159: 194-204. PMID 21782315; PMC3169180.
Moon CP and Fleming KG (2011) “From the Cover: Side-chain hydrophobicity scale derived from transmembrane protein folding in lipid bilayers” PNAS 108: 10174-10177. PMID 21606332;
Commentary by Janice L. Robertson
“We choose to go to the membrane” PNAS (2011) 108(25) 10027-10028.
Moon CP and KG Fleming (2011) “Using tryptophan fluorescence to measure the stability of membrane proteins folded in liposomes” Methods Enzymol. Biothermodynamics, Part D 492: 189-211. PMID 21333792;
Burgess, N.K., T.P. Dao, A.M. Stanley, and K.G. Fleming. (2008) Beta-barrel proteins that reside in the E. coli outer membrane in vivo demonstrate varied folding behavior in vitro. J. Biol. Chem. 283:26748-26758.
Mackenzie, K.R., and K.G. Fleming. (2008) Association energetics of membrane spanning alpha-helices. Curr. Opin. Struct. Biol. 18:412-419.
Stanley, A.M., and K.G. Fleming. (2008) The process of folding proteins into membranes: challenges and progress. Arch. Biochem. Biophys. 469:46-66.
Burgess, N.K., A.M. Stanley, and K.G. Fleming. (2008) Determination of membrane protein molecular weights and association equilibrium constants using sedimentation equilibrium and sedimentation velocity. Methods Cell Biol. 84:181-211.
Duong, M.T., T.M. Jaszewski, K.G. Fleming, and K.R. Mackenzie. (2007) Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. J. Mol. Biol. May 18 [Epub ahead of print]
Stanley, A.M., and K.G. Fleming. (2007) The role of a hydrogen bonding network in the transmembrane beta-barrel OMPLA. J. Mol. Biol. 370:912-924.
Stanley, A.M., A.M. Treubrodt, P. Chuawong, T.L. Hendrickson, and K.G. Fleming. (2007) Lipid chain selectivity by outer membrane phospholipase A. J. Mol. Biol. 366:461-468.
Ebie, A.Z., and K.G. Fleming. (2007) Dimerization of the erythropoietin receptor transmembrane domain in micelles. J. Mol. Biol. 366:517-524.
Stanley, A.M., P. Chuawong, T.L. Hendrickson, and K.G. Fleming. (2006) Energetics of outer membrane phospholipase A (OMPLA) dimerization. J. Mol. Biol. 358:120-131.
Kroch, A.E., and K.G. Fleming. (2006) Alternate interfaces may mediate homomeric and heteromeric assembly in the transmembrane domains of SNARE proteins. J. Mol. Biol. 357:184-94.
Fleming, K.G. (2005) Analysis of membrane proteins using analytical ultracentrifugation. (Invited book chapter) Analytical Ultracentrifugation, Techniques and Methods, (Scott DJ, Harding SE, & Rowe AJ, Eds.) Royal Society of Chemistry Publishing, Cambridge, UK.
Stanley, A.M. and K.G. Fleming. (2005) The transmembrane domains of the ErbB receptors do not dimerize strongly in micelles. J. Mol. Biol. 347:759-772.
Kobus, F.J. and K.G. Fleming. (2005) The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions. Biochemistry 44:1464-1470.
Doura, A.K. and K.G. Fleming. (2004) Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer. J. Mol. Biol. 343:1487-1497.
Raasi, S., I. Orlov, K.G. Fleming and C.M. Pickart. (2004) Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A. J. Mol. Biol. 341:1367-1379.
Doura, A.K., F.J. Kobus, L. Dubrovsky, E. Hibbard and K.G. Fleming. (2004) Sequence context modulates the stability of a GxxxG mediated transmembrane helix-helix dimer. J. Mol. Biol. 341:991-998.
Fleming, K.G., C.C. Ren, A.K. Doura, F.J. Kobus, M.E. Eisley and A.M. Stanley. (2004) Thermodynamics of glycophorin A transmembrane helix-helix association in C14 betaine micelles. Biophys. Chem. 108:43-49.
Fleming, K.G. (2002) Standardizing the free energy change of transmembrane helix-helix interactions. J. Mol. Biol. 323:563-571.
Vergis, J.M., K.G. Bulock, K.G. Fleming and G.P. Beardsley. (2001) Human AICAR transformylase/IMP cyclohydrolase: A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity. J. Biol. Chem. 276:7727-7733.
Trombetta, E.S., K.G. Fleming and A. Helenius. (2001) Quaternary and domain structure of glycoprotein processing glucosidase II. Biochemistry 40:10717-10722.
Fleming, K.G. and D.M. Engelman. (2001) Specificity in transmembrane helix-helix interactions defines a hierarchy of stability for sequence variants. Proc. Natl. Acad. Sci. USA 98:14340-14344.
Fleming, K.G., and D.M. Engelman. (2001) Computation and mutagenesis suggest a right-handed structure for the synaptobrevin transmembrane dimer. Proteins 45:313-317.