| Selected Papers |
Dzwolak W, “Vortex-Induced Chiral Bifurcation in Aggregating Insulin” Chirality 22 (2010) E154–E160. Fulara A, Dzwolak W, “Bifurcated Hydrogen Bonds Stabilize Fibrils of Poly(L-glutamic) Acid” J. Phys. Chem. B 114 (2010) 8278–8283. Loksztejn A, Dzwolak W, "Vortex-Induced Formation of Insulin Amyloid Superstructures Probed by Time-Lapse Atomic Force Microscopy and Circular Dichroism Spectroscopy” J. Mol. Biol. 395 (2010) 643–655. Loksztejn A, Dzwolak W, „Noncooperative dimethyl sulfoxide-induced dissection of insulin fibrils: toward soluble building blocks of amyloid” Biochemistry 48 (2009) 4846-4851. Fulara A, Wójcik S, Loksztejn A, Dzwolak W, „De novo refolding and aggregation of insulin in a nonaqueous environment: An inside out protein remake” J. Phys. Chem. B 112 (2008) 8744-8747. Loksztejn, A, Dzwolak, W, “Chiral bifurcation in aggregating insulin: An induced circular dichroism study” J. Mol. Biol., 379 (2008) 9-16. Dzwolak W, Loksztejn A, Galinska-Rakoczy A, Adachi R, Goto Y, Rupnicki L, “Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin” J. Amer. Chem. Soc. 129 (2007) 7517-7522. Dzwolak W “Insulin amyloid fibrils form an inclusion complex with molecular iodine: a misfolded protein as a nanoscale scaffold” Biochemistry 46 (2007) 1568-1572. Dzwolak W, Loksztejn A, Smirnovas V, “New insights into the self-assembly of insulin amyloid fibrils: an H-D exchange FT-IR study” Biochemistry 45 (2006) 8143-8151. Smirnovas, V, Winter, R, Funck, T, and Dzwolak, W, “Protein amyloidogenesis in the context of volume fluctuations: an insulin case study”, ChemPhysChem 7 (2006) 1046-1049. Dzwolak W, Grudzielanek S, Smirnovas V, Ravindra R, Nicolini C, Jansen R, Loksztejn A, Porowski S, Winter R “Ethanol-perturbed amyloidogenic self-assembly of insulin: looking for origins of amyloid strains” Biochemistry 44 (2005) 8948-8958. Smirnovas V, Winter R, Funck T, Dzwolak W, “Thermodynamic properties underlying the alpha-helix-to-beta-sheet transition, aggregation, and amyloidogenesis of polylysine as probed by calorimetry, densimetry, and ultrasound velocimetry” J. Phys. Chem. B 109 (2005) 19043-19045. Dzwolak W, Marszalek PE, “Zipper-like properties of [poly(L-lysine)+poly(L-glutamicacid)] beta-pleated molecular self-assembly” Chem. Commun. 44 (2005) 5557-5559. Jansen R, Dzwolak W, Winter R “Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy” Biophys. J. 88 (2005) 1344-1353. Winter R, Dzwolak W “Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins” Phil. Trans. R. Soc. A 363 (2005) 537-562. Dzwolak W, Smirnovas V, Jansen R, Winter R “Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study” Protein Sci. 13 (2004) 1927-1932, Dzwolak W, Ravindra R, Nicolini C, Jansen R, Winter R “The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of beta-sheet aggregates” J. Amer. Chem. Soc. 126 (2004) 3762-3768, Dzwolak W, Muraki T, Kato M, Taniguchi Y „Chain-length dependence of alpha-helix to beta-sheet transition in polylysine: model of protein aggregation studied by temperature-tuned FT-IR spectroscopy” Biopolymers, 73 (2004) 463-469, Jansen R, Grudzielanek S, Dzwolak W, Winter R, “High pressure promotes circularly shaped insulin amyloid” J. Mol. Biol., 338 (2004) 203-206, Dzwolak W, Ravindra R, Lendermann J, Winter R „Aggregation of bovine insulin probed by DSC/PPC calorimetry and FT-IR spectroscopy” Biochemistry 42 (2003) 11347-11355, |