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, & Seelig, Anna. (2025). Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models [Journal-article]. The Journal of Physical Chemistry B, 129(4), 1229–1236. https://doi.org/10.1021/acs.jpcb.4c07703
, & Seelig, Anna. (2025). Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models [Journal-article]. The Journal of Physical Chemistry B, 129(4), 1229–1236. https://doi.org/10.1021/acs.jpcb.4c07703
, & Seelig, Anna. (2023). Protein Unfolding-Thermodynamic Perspectives and Unfolding Models. International journal of molecular sciences, 24(6), 5457. https://doi.org/10.3390/ijms24065457
, & Seelig, Anna. (2023). Protein Unfolding-Thermodynamic Perspectives and Unfolding Models. International journal of molecular sciences, 24(6), 5457. https://doi.org/10.3390/ijms24065457
, & Seelig, Anna. (2023). Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models. Journal of Physical Chemistry B, 127(15), 3352–3363. https://doi.org/10.1021/acs.jpcb.3c00882
, & Seelig, Anna. (2023). Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models. Journal of Physical Chemistry B, 127(15), 3352–3363. https://doi.org/10.1021/acs.jpcb.3c00882
, & Seelig, Anna. (2023). Chemical Protein Unfolding - A Simple Cooperative Model. Journal of Physical Chemistry B, 127(39), 8296–8304. https://doi.org/10.1021/acs.jpcb.3c03558
, & Seelig, Anna. (2023). Chemical Protein Unfolding - A Simple Cooperative Model. Journal of Physical Chemistry B, 127(39), 8296–8304. https://doi.org/10.1021/acs.jpcb.3c03558
, & Seelig, Anna. (2022). Protein unfolding. Thermodynamic perspectives and unfolding models. bioRxiv. https://doi.org/10.1101/2022.11.08.515403
, & Seelig, Anna. (2022). Protein unfolding. Thermodynamic perspectives and unfolding models. bioRxiv. https://doi.org/10.1101/2022.11.08.515403
, & Seelig, Anna. (2021). Molecular Understanding of Calorimetric Protein Unfolding Experiments. Biophysical Reports, 2(1), 100037. https://doi.org/10.1016/j.bpr.2021.100037
, & Seelig, Anna. (2021). Molecular Understanding of Calorimetric Protein Unfolding Experiments. Biophysical Reports, 2(1), 100037. https://doi.org/10.1016/j.bpr.2021.100037
Garidel, Patrick, Eiperle, Andrea, Blech, Michaela, & . (2020). Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory. Biophysical Journal, 118(5), 1067–1075. https://doi.org/10.1016/j.bpj.2019.12.037
Garidel, Patrick, Eiperle, Andrea, Blech, Michaela, & . (2020). Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory. Biophysical Journal, 118(5), 1067–1075. https://doi.org/10.1016/j.bpj.2019.12.037
Li-Blatter, Xiaochun, & . (2019). Thermal and Chemical Unfolding of Lysozyme. Multistate Zimm-Bragg Theory Versus Two-State Model. The Journal of Physical Chemistry. B, 123(48), 10181–10191. https://doi.org/10.1021/acs.jpcb.9b08816
Li-Blatter, Xiaochun, & . (2019). Thermal and Chemical Unfolding of Lysozyme. Multistate Zimm-Bragg Theory Versus Two-State Model. The Journal of Physical Chemistry. B, 123(48), 10181–10191. https://doi.org/10.1021/acs.jpcb.9b08816
. (2018). Titration Calorimetry and Differential Scanning Calorimetry of Lipid-Protein Interactions. In Wilhelm, Emmerich; Letcher, Trevor M. (Ed.), Enthalpy and Internal Energy. Liquids, Solutions and Vapours (pp. 299–314). Royal Society of Chemistry. https://doi.org/10.1039/9781788010214
. (2018). Titration Calorimetry and Differential Scanning Calorimetry of Lipid-Protein Interactions. In Wilhelm, Emmerich; Letcher, Trevor M. (Ed.), Enthalpy and Internal Energy. Liquids, Solutions and Vapours (pp. 299–314). Royal Society of Chemistry. https://doi.org/10.1039/9781788010214
Eckhardt, D., Li-Blatter, X., Schönfeld, H.-J., Heerklotz, H., & (2018). Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation. Biophysical Chemistry, 240, 42–49. https://doi.org/10.1016/j.bpc.2018.05.005
Eckhardt, D., Li-Blatter, X., Schönfeld, H.-J., Heerklotz, H., & (2018). Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation. Biophysical Chemistry, 240, 42–49. https://doi.org/10.1016/j.bpc.2018.05.005
. (2018). Cooperative protein unfolding. A statistical-mechanical model for the action of denaturants. Biophysical Chemistry, 233, 19–25. https://doi.org/10.1016/j.bpc.2017.12.001
. (2018). Cooperative protein unfolding. A statistical-mechanical model for the action of denaturants. Biophysical Chemistry, 233, 19–25. https://doi.org/10.1016/j.bpc.2017.12.001
Assmus, Frauke, Ross, Alfred, Fischer, Holger, , & Seelig, Anna. (2017). (31)P and (1)H NMR Studies of the Molecular Organization of Lipids in the Parallel Artificial Membrane Permeability Assay. Molecular Pharmaceutics, 14(1), 284–295. https://doi.org/10.1021/acs.molpharmaceut.6b00889
Assmus, Frauke, Ross, Alfred, Fischer, Holger, , & Seelig, Anna. (2017). (31)P and (1)H NMR Studies of the Molecular Organization of Lipids in the Parallel Artificial Membrane Permeability Assay. Molecular Pharmaceutics, 14(1), 284–295. https://doi.org/10.1021/acs.molpharmaceut.6b00889
Schönfeld, Hans-Joachim, Roessner, Dierk, & . (2016). Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering. Journal of Physical Chemistry B, 120(7), 35–1228. https://doi.org/10.1021/acs.jpcb.5b12397
Schönfeld, Hans-Joachim, Roessner, Dierk, & . (2016). Self-Association of Apo A-1 Studied with Dynamic and Static Light Scattering. Journal of Physical Chemistry B, 120(7), 35–1228. https://doi.org/10.1021/acs.jpcb.5b12397
, & Schönfeld, Hans-Joachim. (2016). Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding. Quarterly Reviews of Biophysics, 49, e9. https://doi.org/10.1017/s0033583516000044
, & Schönfeld, Hans-Joachim. (2016). Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding. Quarterly Reviews of Biophysics, 49, e9. https://doi.org/10.1017/s0033583516000044
Schulthess, Therese, Schönfeld, Hans-Joachim, & . (2015). Thermal unfolding of apolipoprotein a-1 : evaluation of methods and models. Biochemistry, 54(19), 75–3063. https://doi.org/10.1021/acs.biochem.5b00238
Schulthess, Therese, Schönfeld, Hans-Joachim, & . (2015). Thermal unfolding of apolipoprotein a-1 : evaluation of methods and models. Biochemistry, 54(19), 75–3063. https://doi.org/10.1021/acs.biochem.5b00238
Voievoda, Nataliia, Schulthess, Therese, Bechinger, Burkhard, & . (2015). Thermodynamic and Biophysical Analysis of the Membrane-Association of a Histidine-Rich Peptide with Efficient Antimicrobial and Transfection Activities. Journal of Physical Chemistry B, 119(30), 87–9678. https://doi.org/10.1021/acs.jpcb.5b04543
Voievoda, Nataliia, Schulthess, Therese, Bechinger, Burkhard, & . (2015). Thermodynamic and Biophysical Analysis of the Membrane-Association of a Histidine-Rich Peptide with Efficient Antimicrobial and Transfection Activities. Journal of Physical Chemistry B, 119(30), 87–9678. https://doi.org/10.1021/acs.jpcb.5b04543
Schmidt, Annika, Belaaouaj, Azzaq, Bissinger, Rosi, Koller, Garrit, Malleret, Laurette, D’Orazio, Ciro, Facchinelli, Martino, Schulte-Hubbert, Bernhard, Molinaro, Antonio, Holst, Otto, Hammermann, Jutta, Schniederjans, Monika, Meyer, Keith C., Damkiaer, Soeren, Piacentini, Giorgio, Assael, Baroukh, Bruce, Kenneth, Häußler, Susanne, LiPuma, John J., et al. (2014). Neutrophil elastase-mediated increase in airway temperature during inflammation. Journal of Cystic Fibrosis, 13(6), 31–623. https://doi.org/10.1016/j.jcf.2014.03.004
Schmidt, Annika, Belaaouaj, Azzaq, Bissinger, Rosi, Koller, Garrit, Malleret, Laurette, D’Orazio, Ciro, Facchinelli, Martino, Schulte-Hubbert, Bernhard, Molinaro, Antonio, Holst, Otto, Hammermann, Jutta, Schniederjans, Monika, Meyer, Keith C., Damkiaer, Soeren, Piacentini, Giorgio, Assael, Baroukh, Bruce, Kenneth, Häußler, Susanne, LiPuma, John J., et al. (2014). Neutrophil elastase-mediated increase in airway temperature during inflammation. Journal of Cystic Fibrosis, 13(6), 31–623. https://doi.org/10.1016/j.jcf.2014.03.004
Domingues, Tatiana M., Mattei, Bruno, , Perez, Katia R., Miranda, Antonio, & Riske, Karin A. (2013). Interaction of the antimicrobial Peptide gomesin with model membranes : a calorimetric study. Langmuir, 29(27), 18–8609. https://doi.org/10.1021/la401596s
Domingues, Tatiana M., Mattei, Bruno, , Perez, Katia R., Miranda, Antonio, & Riske, Karin A. (2013). Interaction of the antimicrobial Peptide gomesin with model membranes : a calorimetric study. Langmuir, 29(27), 18–8609. https://doi.org/10.1021/la401596s
Perspicace, Samantha, Rufer, Arne C., Thoma, Ralf, Müller, Francis, Hennig, Michael, Ceccarelli, Simona, Schulz-Gasch, Tanja, & . (2013). Isothermal titration calorimetry with micelles : thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein. FEBS Open Bio, 3, 11–204. https://doi.org/10.1016/j.fob.2013.04.003
Perspicace, Samantha, Rufer, Arne C., Thoma, Ralf, Müller, Francis, Hennig, Michael, Ceccarelli, Simona, Schulz-Gasch, Tanja, & . (2013). Isothermal titration calorimetry with micelles : thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein. FEBS Open Bio, 3, 11–204. https://doi.org/10.1016/j.fob.2013.04.003
Québatte, Gabriela, Kitas, Eric, & . (2013). riDOM, a Cell-Penetrating Peptide : Interaction with DNA and Heparan Sulfate. Journal of Physical Chemistry B, 117(37), 17–10807. https://doi.org/10.1021/jp404979y
Québatte, Gabriela, Kitas, Eric, & . (2013). riDOM, a Cell-Penetrating Peptide : Interaction with DNA and Heparan Sulfate. Journal of Physical Chemistry B, 117(37), 17–10807. https://doi.org/10.1021/jp404979y
Québatte, Gabriela, Kitas, Eric, & . (2013). riDOM, a cell penetrating peptide : interaction with phospholipid bilayers. BBA - Biochimica et Biophysica Acta, 1838(3), 77–968. https://doi.org/10.1016/j.bbamem.2013.10.017
Québatte, Gabriela, Kitas, Eric, & . (2013). riDOM, a cell penetrating peptide : interaction with phospholipid bilayers. BBA - Biochimica et Biophysica Acta, 1838(3), 77–968. https://doi.org/10.1016/j.bbamem.2013.10.017
Zehender, F, Ziegler, A, Schönfeld, H-J, & . (2012). Thermodynamics of protein self-association and unfolding : the case of apolipoprotein a-I. Biochemistry, 51(6), 80–1269. https://doi.org/10.1021/bi2013799
Zehender, F, Ziegler, A, Schönfeld, H-J, & . (2012). Thermodynamics of protein self-association and unfolding : the case of apolipoprotein a-I. Biochemistry, 51(6), 80–1269. https://doi.org/10.1021/bi2013799
Loew, C., Riske, K. A., Lamy, M. T., & (2011). Thermal Phase Behavior of DMPG as revealed by 2H- and 31P- NMR. Langmuir, 27(16), 9–10041. https://doi.org/10.1021/la201027p
Loew, C., Riske, K. A., Lamy, M. T., & (2011). Thermal Phase Behavior of DMPG as revealed by 2H- and 31P- NMR. Langmuir, 27(16), 9–10041. https://doi.org/10.1021/la201027p
Sauder, Reto, , & Ziegler, André. (2011). Thermodynamics of lipid interactions with cell-penetrating peptides. Methods in Molecular Biology, 683, 55–129. https://doi.org/10.1007/978-1-60761-919-2_10
Sauder, Reto, , & Ziegler, André. (2011). Thermodynamics of lipid interactions with cell-penetrating peptides. Methods in Molecular Biology, 683, 55–129. https://doi.org/10.1007/978-1-60761-919-2_10
Ziegler, Andre, & . (2011). Contributions of Glycosaminoglycan Binding and Clustering to the Biological Uptake of the Nonamphipathic Cell-Penetrating Peptide WR(9). Biochemistry, 50(21), 4650–4664. https://doi.org/10.1021/bi1019429
Ziegler, Andre, & . (2011). Contributions of Glycosaminoglycan Binding and Clustering to the Biological Uptake of the Nonamphipathic Cell-Penetrating Peptide WR(9). Biochemistry, 50(21), 4650–4664. https://doi.org/10.1021/bi1019429
Beck, A., Li-Blatter, X., Seelig, A., & (2010). On the Interaction of Ionic Detergents with Lipid Membranes : Thermodynamic Comparison of n-Alkyl-+N(CH3)3 and n-Alkyl-SO4-. Journal of Physical Chemistry B, 114(48), 15862–15871. https://doi.org/10.1021/jp107088d
Beck, A., Li-Blatter, X., Seelig, A., & (2010). On the Interaction of Ionic Detergents with Lipid Membranes : Thermodynamic Comparison of n-Alkyl-+N(CH3)3 and n-Alkyl-SO4-. Journal of Physical Chemistry B, 114(48), 15862–15871. https://doi.org/10.1021/jp107088d
Meier, Matthias, & . (2010). Lipid and peptide dynamics in membranes upon insertion of n-alkyl-beta-D-glucopyranosides. Biophysical Journal, 98(8), 38–1529. https://doi.org/10.1016/j.bpj.2009.12.4286
Meier, Matthias, & . (2010). Lipid and peptide dynamics in membranes upon insertion of n-alkyl-beta-D-glucopyranosides. Biophysical Journal, 98(8), 38–1529. https://doi.org/10.1016/j.bpj.2009.12.4286
Hayley, Michael, Perspicace, Samantha, Schulthess, Therese, & . (2009). Calcium enhances the proteolytic activity of BACE1 : an in vitro biophysical and biochemical characterization of the BACE1-calcium interaction. Biochimica et Biophysica Acta, 1788(9), 8–1933. https://doi.org/10.1016/j.bbamem.2009.05.015
Hayley, Michael, Perspicace, Samantha, Schulthess, Therese, & . (2009). Calcium enhances the proteolytic activity of BACE1 : an in vitro biophysical and biochemical characterization of the BACE1-calcium interaction. Biochimica et Biophysica Acta, 1788(9), 8–1933. https://doi.org/10.1016/j.bbamem.2009.05.015
Klocek, Gabriela, Schulthess, Therese, Shai, Yechiel, & . (2009). Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation. Biochemistry, 48(12), 96–2586. https://doi.org/10.1021/bi802127h
Klocek, Gabriela, Schulthess, Therese, Shai, Yechiel, & . (2009). Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation. Biochemistry, 48(12), 96–2586. https://doi.org/10.1021/bi802127h
Klocek, Gabriela, & . (2008). Melittin interaction with sulfated cell surface sugars. Biochemistry, 47(9), 9–2841. https://doi.org/10.1021/bi702258z
Klocek, Gabriela, & . (2008). Melittin interaction with sulfated cell surface sugars. Biochemistry, 47(9), 9–2841. https://doi.org/10.1021/bi702258z
Meier, M., & (2008). Length dependence of the coil beta-sheet transition in a membrane environment. Journal of the American Chemical Society, 130(3), 24–1017. https://doi.org/10.1021/ja077231r
Meier, M., & (2008). Length dependence of the coil beta-sheet transition in a membrane environment. Journal of the American Chemical Society, 130(3), 24–1017. https://doi.org/10.1021/ja077231r
Ziegler, André, & . (2008). Binding and clustering of glycosaminoglycans : a common property of mono- and multivalent cell-penetrating compounds. Biophysical Journal, 94(6), 9–2142. https://doi.org/10.1529/biophysj.107.113472
Ziegler, André, & . (2008). Binding and clustering of glycosaminoglycans : a common property of mono- and multivalent cell-penetrating compounds. Biophysical Journal, 94(6), 9–2142. https://doi.org/10.1529/biophysj.107.113472
Brockhaus, M., Ganz, P., Huber, W., Bohrmann, B., Loetscher, H. -R., & (2007). Thermodynamic studies on the interaction of antibodies with beta-amyloid peptide. Journal of Physical Chemistry B, 111(5), 43–1238. https://doi.org/10.1021/jp0664059
Brockhaus, M., Ganz, P., Huber, W., Bohrmann, B., Loetscher, H. -R., & (2007). Thermodynamic studies on the interaction of antibodies with beta-amyloid peptide. Journal of Physical Chemistry B, 111(5), 43–1238. https://doi.org/10.1021/jp0664059
Heerklotz, H., & (2007). Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. European Biophysics Journal, 36(4-5), 14–305. https://doi.org/10.1007/s00249-006-0091-5
Heerklotz, H., & (2007). Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. European Biophysics Journal, 36(4-5), 14–305. https://doi.org/10.1007/s00249-006-0091-5
Kohler, G., Rost, F., & (2007). Simultaneous separation of intracellular and extracellular lactate NMR signals of human erythrocytes. Magnetic Resonance in Medicine, 58(2), 7–213. https://doi.org/10.1002/mrm.21309
Kohler, G., Rost, F., & (2007). Simultaneous separation of intracellular and extracellular lactate NMR signals of human erythrocytes. Magnetic Resonance in Medicine, 58(2), 7–213. https://doi.org/10.1002/mrm.21309
Meier, Matthias, & . (2007). Thermodynamics of the coil beta-sheet transition in a membrane environment. Journal of Molecular Biology, 369(1), 89–277. https://doi.org/10.1016/j.jmb.2007.02.082
Meier, Matthias, & . (2007). Thermodynamics of the coil beta-sheet transition in a membrane environment. Journal of Molecular Biology, 369(1), 89–277. https://doi.org/10.1016/j.jmb.2007.02.082
Ziegler, André, & . (2007). High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA. Biochemistry, 46(27), 45–8138. https://doi.org/10.1021/bi700416h
Ziegler, André, & . (2007). High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA. Biochemistry, 46(27), 45–8138. https://doi.org/10.1021/bi700416h
Gonçalves, Elisabete, Kitas, Eric, & . (2006). Structural and thermodynamic aspects of the interaction between heparan sulfate and analogues of melittin. Biochemistry, 45(9), 94–3086. https://doi.org/10.1021/bi052221t
Gonçalves, Elisabete, Kitas, Eric, & . (2006). Structural and thermodynamic aspects of the interaction between heparan sulfate and analogues of melittin. Biochemistry, 45(9), 94–3086. https://doi.org/10.1021/bi052221t
Honnappa, Srinivas, Jahnke, Wolfgang, , & Steinmetz, Michel O. (2006). Control of intrinsically disordered stathmin by multisite phosphorylation. Journal of Biological Chemistry, 281(23), 83–16078. https://doi.org/10.1074/jbc.m513524200
Honnappa, Srinivas, Jahnke, Wolfgang, , & Steinmetz, Michel O. (2006). Control of intrinsically disordered stathmin by multisite phosphorylation. Journal of Biological Chemistry, 281(23), 83–16078. https://doi.org/10.1074/jbc.m513524200
Meier, M, Blatter, X Li, Seelig, A, & . (2006). Interaction of verapamil with lipid membranes and P-glycoprotein : connecting thermodynamics and membrane structure with functional activity. Biophysical Journal, 91(8), 55–2943. https://doi.org/10.1529/biophysj.106.089581
Meier, M, Blatter, X Li, Seelig, A, & . (2006). Interaction of verapamil with lipid membranes and P-glycoprotein : connecting thermodynamics and membrane structure with functional activity. Biophysical Journal, 91(8), 55–2943. https://doi.org/10.1529/biophysj.106.089581
Gonçalves, Elisabete, Kitas, Eric, & . (2005). Binding of oligoarginine to membrane lipids and heparan sulfate : structural and thermodynamic characterization of a cell-penetrating peptide. Biochemistry, 44(7), 702–2692. https://doi.org/10.1021/bi048046i
Gonçalves, Elisabete, Kitas, Eric, & . (2005). Binding of oligoarginine to membrane lipids and heparan sulfate : structural and thermodynamic characterization of a cell-penetrating peptide. Biochemistry, 44(7), 702–2692. https://doi.org/10.1021/bi048046i
Ziegler, André, Nervi, Pierluigi, Dürrenberger, Markus, & . (2005). The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblast : optical, biophysical, and metabolic evidence. Biochemistry, 44(1), 48–138. https://doi.org/10.1021/bi0491604
Ziegler, André, Nervi, Pierluigi, Dürrenberger, Markus, & . (2005). The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblast : optical, biophysical, and metabolic evidence. Biochemistry, 44(1), 48–138. https://doi.org/10.1021/bi0491604
Anderson, Thomas G, Tan, Anmin, Ganz, Peter, & . (2004). Calorimetric measurement of phospholipid interaction with methyl-beta-cyclodextrin. Biochemistry, 43(8), 61–2251. https://doi.org/10.1021/bi0358869
Anderson, Thomas G, Tan, Anmin, Ganz, Peter, & . (2004). Calorimetric measurement of phospholipid interaction with methyl-beta-cyclodextrin. Biochemistry, 43(8), 61–2251. https://doi.org/10.1021/bi0358869
Heerklotz, Heiko, Wieprecht, Torsten, & . (2004). Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. Journal of Physical Chemistry B, 108(15), 4909–4915. https://doi.org/10.1021/jp0371938
Heerklotz, Heiko, Wieprecht, Torsten, & . (2004). Membrane perturbation by the lipopeptide surfactin and detergents as studied by deuterium NMR. Journal of Physical Chemistry B, 108(15), 4909–4915. https://doi.org/10.1021/jp0371938
Schwarz, R., , & Kunnecke, B. (2004). Structural properties of perfluorinated linear alkanes : a 19F and 13C NMR study of perfluorononane. Magnetic Resonance in Chemistry, 42(6), 7–512. https://doi.org/10.1002/mrc.1380
Schwarz, R., , & Kunnecke, B. (2004). Structural properties of perfluorinated linear alkanes : a 19F and 13C NMR study of perfluorononane. Magnetic Resonance in Chemistry, 42(6), 7–512. https://doi.org/10.1002/mrc.1380
. (2004). Thermodynamics of lipid-peptide interactions. Biochimica et Biophysica Acta, 1666(1-2), 40–50. https://doi.org/10.1016/j.bbamem.2004.08.004
. (2004). Thermodynamics of lipid-peptide interactions. Biochimica et Biophysica Acta, 1666(1-2), 40–50. https://doi.org/10.1016/j.bbamem.2004.08.004
Ziegler, André, & . (2004). Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate : binding mechanism and thermodynamic parameters. Biophysical Journal, 86(1 Pt 1), 63–254. https://doi.org/10.1016/s0006-3495(04)74101-6
Ziegler, André, & . (2004). Interaction of the protein transduction domain of HIV-1 TAT with heparan sulfate : binding mechanism and thermodynamic parameters. Biophysical Journal, 86(1 Pt 1), 63–254. https://doi.org/10.1016/s0006-3495(04)74101-6
Bilecen, D., Schulte, A. -C., Kaspar, A., Kustermann, E., , Elverfeldt, D., & Scheffler, K. (2003). Detection of the non-steroidal anti-inflammatory drug niflumic acid in humans : a combined 19F-MRS in vivo and in vitro study. NMR in Biomedicine, 16(3), 51–144. https://doi.org/10.1002/nbm.820
Bilecen, D., Schulte, A. -C., Kaspar, A., Kustermann, E., , Elverfeldt, D., & Scheffler, K. (2003). Detection of the non-steroidal anti-inflammatory drug niflumic acid in humans : a combined 19F-MRS in vivo and in vitro study. NMR in Biomedicine, 16(3), 51–144. https://doi.org/10.1002/nbm.820
Heerklotz, Heiko, Szadkowska, Halina, Anderson, Thomas, & . (2003). The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. Journal of Molecular Biology, 329(4), 9–793. https://doi.org/10.1016/s0022-8236(03)00504-7
Heerklotz, Heiko, Szadkowska, Halina, Anderson, Thomas, & . (2003). The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. Journal of Molecular Biology, 329(4), 9–793. https://doi.org/10.1016/s0022-8236(03)00504-7
Honnappa, S, Cutting, B, Jahnke, W, , & Steinmetz, MO. (2003). Thermodynamics of the Op18/stathmin-tubulin interaction. Journal of Biological Chemistry, 278(40), 38926–38934. https://doi.org/10.1074/jbc.m305546200
Honnappa, S, Cutting, B, Jahnke, W, , & Steinmetz, MO. (2003). Thermodynamics of the Op18/stathmin-tubulin interaction. Journal of Biological Chemistry, 278(40), 38926–38934. https://doi.org/10.1074/jbc.m305546200
Karelson, G., Ziegler, A., Kunnecke, B., & (2003). Feeding versus infusion : a novel approach to study the NAA metabolism in rat brain. NMR in Biomedicine, 16(6-7), 23–413. https://doi.org/10.1002/nbm.845
Karelson, G., Ziegler, A., Kunnecke, B., & (2003). Feeding versus infusion : a novel approach to study the NAA metabolism in rat brain. NMR in Biomedicine, 16(6-7), 23–413. https://doi.org/10.1002/nbm.845
Machaidze, Gia, & . (2003). Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine : Comparison between micellar and membrane environments. Biochemistry, 42(43), 6–12570. https://doi.org/10.1021/bi035225b
Machaidze, Gia, & . (2003). Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine : Comparison between micellar and membrane environments. Biochemistry, 42(43), 6–12570. https://doi.org/10.1021/bi035225b
Ziegler, André, Blatter, Xiaochun Li, Seelig, Anna, & . (2003). Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles : binding mechanism and thermodynamic analysis. Biochemistry, 42(30), 94–9185. https://doi.org/10.1021/bi0346805
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