TY - GEN A1 - Best, Robert B. A1 - Zheng, Wenwei A1 - Borgia, Alessandro A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Schuler, Benjamin T1 - Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water" T2 - Science N2 - Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction. Y1 - 2018 U6 - https://doi.org/10.1126/science.aar7101 SN - 0036-8075 SN - 1095-9203 VL - 361 IS - 6405 PB - American Assoc. for the Advancement of Science CY - Washington ER - TY - BOOK A1 - Jeske, Janin A1 - Brehmer, Bastian A1 - Menge, Falko A1 - Hüttenrauch, Stefan A1 - Adam, Christian A1 - Schüler, Benjamin A1 - Schult, Wolfgang A1 - Rasche, Andreas A1 - Polze, Andreas T1 - Aspektorientierte Programmierung : Überblick über Techniken und Werkzeuge T3 - Technische Berichte des Hasso-Plattner-Instituts für Softwaresystemtechnik an der Universität Potsda Y1 - 2006 SN - 3-939469-23-8 SN - 1613-5652 VL - 14 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - JOUR A1 - Buscaglia, Marco A1 - Schuler, Benjamin A1 - Lapidus, Lisa J. A1 - Eaton, Wiliam A. A1 - Hofrichter, James T1 - Kinetics of intramolecular contact formation in a denatured protein N2 - Quenching of the triplet state of tryptophan by cysteine has provided a new tool for measuring the rate of forming a specific intramolecular contact in disordered polypeptides. Here, we use this technique to investigate contact formation in the denatured state of CspTm, a small cold-shock protein from Thermotoga maritima, engineered to contain a single tryptophan residue (W29) and a single cysteine residue at the C terminus (C67). At all concentrations of denaturant, the decay rate of the W29 triplet of the unfolded protein is more than tenfold faster than the rate observed for the native protein (not, vert, similar104 s;1). Experiments on the unfolded protein without the added C- terminal cysteine residue show that this faster rate results entirely from contact quenching by C67. The quenching rate in the unfolded state by C67 increases at concentrations of denaturant that favor folding, indicating a compaction of the unfolded protein as observed previously in single-molecule Foerster resonance energy transfer (FRET) experiments. Y1 - 2003 UR - http://www.sciencedirect.com/science/article/pii/S002228360300891X SN - 0022-2836 ER - TY - JOUR A1 - Goetz, C. A1 - Suopanki, J. A1 - Schuler, Benjamin A1 - Wanker, E. A1 - Herrmann, Andreas T1 - Perturbation of brain lipid membrane by soluble Huntingtin depends on its polyproline tract Y1 - 2005 SN - 0006-3495 ER - TY - JOUR A1 - Schuler, Benjamin A1 - Lipman, Everett A. A1 - Steinbach, P. J. A1 - Kumke, Michael Uwe A1 - Eaton, W. A. T1 - Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence N2 - To determine whether Forster resonance energy transfer (FRET) measurements can provide quantitative distance information in single-molecule fluorescence experiments on polypeptides, we measured FRET efficiency distributions for donor and acceptor dyes attached to the ends of freely diffusing polyproline molecules of various lengths. The observed mean FRET efficiencies agree with those determined from ensemble lifetime measurements but differ considerably from the values expected from Forster theory, with polyproline treated as a rigid rod. At donor-acceptor distances much less than the Forster radius R-o, the observed efficiencies are lower than predicted, whereas at distances comparable to and greater than R-0, they are much higher. Two possible contributions to the former are incomplete orientational averaging during the donor lifetime and, because of the large size of the dyes, breakdown of the point-dipole approximation assumed in Forster theory. End-to-end distance distributions and correlation times obtained from Langevin molecular dynamics simulations suggest that the differences for the longer polyproline peptides can be explained by chain bending, which considerably shortens the donor-acceptor distances Y1 - 2005 SN - 0027-8424 ER - TY - JOUR A1 - Rhoades, E. A1 - Cohen, M. A1 - Gussakovsky, E. A1 - Schuler, Benjamin A1 - Haran, G. T1 - Single molecule protein folding Y1 - 2004 SN - 0006-3495 ER - TY - BOOK A1 - Adam, Christian A1 - Brehmer, Bastian A1 - Hüttenrauch, Stefan A1 - Jeske, Janin A1 - Polze, Andreas A1 - Rasche, Andreas A1 - Schüler, Benjamin A1 - Schult, Wolfgang T1 - Aspektorientierte Programmierung : Überblick über Techniken und Werkzeuge N2 - Inhaltsverzeichnis 1 Einführung 2 Aspektorientierte Programmierung 2.1 Ein System als Menge von Eigenschaften 2.2 Aspekte 2.3 Aspektweber 2.4 Vorteile Aspektorientierter Programmierung 2.5 Kategorisierung der Techniken und Werkzeuge f ¨ ur Aspektorientierte Programmierung 3 Techniken und Werkzeuge zur Analyse Aspektorientierter Softwareprogramme 3.1 Virtual Source File 3.2 FEAT 3.3 JQuery 3.4 Aspect Mining Tool 4 Techniken und Werkzeuge zum Entwurf Aspektorientierter Softwareprogramme 4.1 Concern Space Modeling Schema 4.2 Modellierung von Aspekten mit UML 4.3 CoCompose 4.4 Codagen Architect 5 Techniken und Werkzeuge zur Implementierung Aspektorientierter Softwareprogramme 5.1 Statische Aspektweber 5.2 Dynamische Aspektweber 6 Zusammenfassung T3 - Technische Berichte des Hasso-Plattner-Instituts für Digital Engineering an der Universität Potsdam - 14 Y1 - 2006 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-33796 SN - 978-3-939469-23-0 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - GEN A1 - Schuler, Benjamin A1 - Lipman, Everett A. A1 - Steinbach, Peter J. A1 - Kumke, Michael Uwe A1 - Eaton, William A. T1 - Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence N2 - To determine whether Förster resonance energy transfer (FRET) measurements can provide quantitative distance information in single-molecule fluorescence experiments on polypeptides, we measured FRET efficiency distributions for donor and acceptor dyes attached to the ends of freely diffusing polyproline molecules of various lengths. The observed mean FRET efficiencies agree with those determined from ensemble lifetime measurements but differ considerably from the values expected from Förster theory, with polyproline treated as a rigid rod. At donor–acceptor distances much less than the Förster radius R0, the observed efficiencies are lower than predicted, whereas at distances comparable to and greater than R0, they are much higher. Two possible contributions to the former are incomplete orientational averaging during the donor lifetime and, because of the large size of the dyes, breakdown of the point-dipole approximation assumed in Förster theory. End-to-end distance distributions and correlation times obtained from Langevin molecular dynamics simulations suggest that the differences for the longer polyproline peptides can be explained by chain bending, which considerably shortens the donor–acceptor distances. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - paper 008 KW - Förster resonance energy transfer KW - molecular dynamics KW - polypeptide KW - FRET Y1 - 2005 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-12229 ER - TY - JOUR A1 - Hoffmann, Armin S. A1 - Kane, Avinash S. A1 - Nettels, Daniel A1 - Hertzog, David E. A1 - Baumgärtel, Peter A1 - Lengefeld, Jan A1 - Reichardt, Gerd A1 - Horsley, David A. A1 - Seckler, Robert A1 - Bakajin, Olgica A1 - Schuler, Benjamin T1 - Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy Y1 - 2007 UR - http://www.mendeley.com/research/mapping-protein-collapse-with-singlemolecule-fluorescence-and-kinetic- synchrotron-radiation-circular-dichroism-spectroscopy/# SN - 0027-8424 ER - TY - JOUR A1 - Nettels, Daniel A1 - Müller-Späth, Sonja A1 - Küster, Frank A1 - Hofmann, Hagen A1 - Haenni, Domminik A1 - Rüegger, Stefan A1 - Reymond, Luc A1 - Hoffmann, Armin S. A1 - Kubelka, Jan A1 - Heinz, Benjamin A1 - Gast, Klaus A1 - Best, Robert B. A1 - Schuler, Benjamin T1 - Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins N2 - We used single-molecule FRET in combination with other biophysical methods and molecular simulations to investigate the effect of temperature on the dimensions of unfolded proteins. With singlemolecule FRET, this question can be addressed even under nearnative conditions, where most molecules are folded, allowing us to probe a wide range of denaturant concentrations and temperatures. We find a compaction of the unfolded state of a small cold shock protein with increasing temperature in both the presence and the absence of denaturant, with good agreement between the results from single-molecule FRET and dynamic light scattering. Although dissociation of denaturant from the polypeptide chain with increasing temperature accounts for part of the compaction, the results indicate an important role for additional temperaturedependent interactions within the unfolded chain. The observation of a collapse of a similar extent in the extremely hydrophilic, intrinsically disordered protein prothymosin suggests that the hydrophobic effect is not the sole source of the underlying interactions. Circular dichroism spectroscopy and replica exchange molecular dynamics simulations in explicit water show changes in secondary structure content with increasing temperature and suggest a contribution of intramolecular hydrogen bonding to unfolded state collapse. Y1 - 2009 UR - http://www.pnas.org/content/106/49/20740.full.pdf+html SN - 0027-8424 ER -