Martin Luther University Halle-Wittenberg

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Journalpublikationen:

67. Klepsch, M.M., Kovermann, M., Löw, C., Balbach, J., Permentier, H.P., Fusetti, F., de Gier, J.W., Slotboom, D.J., Berntsson, R.P. (2011), J. Mol. Biol., in press

"Escherichia coli peptide binding OppA has a preference for positively charged peptides."

66. Sachs, R., Max, K.E.A., Heinemann, U., Balbach, J. (2011), RNA, in press

"RNA single-strands bind to a conserved surface of the major cold shock protein in crystals and solution."

65. Casares-Atienza, S., Weininger, U., Camara-Artigas, A., Balbach, J., Carcia-Mira, M.M. (2011), Biophys. Chem., 159, 267-274.

"Three-state thermal unfolding of onconase."

64. Haupt, C., Weininger, U., Kovermann, M., Balbach, J. (2011), Biochemistry, 40, 7321-7329.

"Local and Coupled Thermodynamic Stability of the Two-Domain and Bifunctional Enzyme SlyD from Escherichia coli."

63. Kahra, D., Kovermann, M., Löw, C., Hirschfeld, V., Haupt, C., Balbach, J., Hübner, C.G. (2011), J. Mol. Biol., 411, 781-790.

"Conformational plasticity and dynamics in the generic protein folding catalst SlyD unraveled by single-molecule FRET."

62. Haupt, C., Patzschke, R., Weininger, U., Gröger, S., Kovermann, M., Balbach, J. (2011), J. Am. Chem. Soc., 133, 11154-11162.

"Transient Enzyme-Substrate Recognition Monitored by Real-Time NMR."

61. Garvey, M., Tepper, K., Haupt, C., Knüpfer, U., Klement, K., Meinhardt, J., Horn, U., Balbach, J., Fändrich, M. (2011), Biochem. Biophys. Res. Commun., 409, 385-388.

"Phophate and HEPES buffers potently effect the fibrillation and oligomerization mechanism of Alzheimer's A&beta peptide."

60. Kovermann, M., Zierold, R., Haupt, C., Löw, C., Balbach, J. (2011), Biochem. Biophys. Acta, 1814, 873-881.

"NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD."

59. Theisgen, S., Thomas, L., Schröder, T., Lange, C., Kovermann, M., Balbach, J., Huster, D. (2011), Eur. Biophys. J., 40, 565-576.

"The presence of membranes or micelles induces structural chenges of the myristoylated guanylate cyclase activating protein 2."

58. Drechsler, N., Fröbel, J., Jahreis, G., Gobalswamy, M., Balbach, J., Bosse-Doenecke, Rudolph., R. (2011), Biophys. Chem., 154, 66-72.

"Binding specifity of the ectodomain of the parathyroid hormone receptor."

57. Lorenz, S.H., jakob, R.P., Weininger, U., Balbach, J., Dobbek, H., Schmid, F.X. (2011), J. Mol. Biol., 405, 989-1003.

"The filamentous phages fd and IF1 use different mechanisms to infect Escherichia coli."

56. Lilie, H., Bär, D., Kettner, K., Weininger, U., Balbach, J., Naumann, M., Müller, E.C., Otto, A., Gast, K., Golbik, R., Kriegel, T. (2011), PEDS, 24, 79-87.

"Yeast hexokinase isoenzyme ScHxk2: stability of a two-domain protein with discontinuous domains."

55. Herbst, F., Schröter, K., Gunkel, I., Gröger, S., Thurn-Albrecht, T., Balbach, J., Binder, W.H. (2010), Macromolecules, 43, 100006-10016.

"Aggregation and Chain Dynamics in Supramolecular Polymers by Dynamic Rheology: Cluster Formation and Self-Aggregation."

54. Dahse, K., Garvey, M., Kovermann, M., Vogel, A., Balbach, J., Fändrich, M., Fahr, A. (2010), J. Mol. Biol., 403, 643-659.

"DHPC strongly affects the structure and oligomerization propensity of Alzheimer's A&beta(1-40) peptide."

53. Jakob, R.P., Zierer, B.K., Weininger, U., Hofmann, S.D., Lorenz, S.H., Balbach, J., Dobbek, H., Schmid, F.X. (2010), J. Mol. Biol., 399, 331-346.

"Elimination of a cis-Proline-Containing Loop and Turn Optimization stabilizes a Protein and Accelerates Its Folding."

52. Löw, C., Neumann, P., Tidow, H., Weininger, U., Haupt, C., Friedrich-Epler, B., Scholz, C., Stubbs, M.T., Balbach, J. (2010), J. Mol. Biol., 398, 375-390.

"Crystal Structure Determination and Functional Characterization of the Metallochaperone SlyD from Thermus thermophilus."

51. Schulenburg, C., Weininger, U., Neumann, P., Meiselbach, H., Stubbs, M.T., Sticht, H., Balbach, J., Ulbrich-Hoffmann, R., Arnold, U. (2010), ChemBioVhem, 11, 978-986.

"Impact of the C-terminal disulfide bond on the folding and stability of onconase."

50. Weininger, U., Jakob, R.P., Kovermann, M., Balbach, J., Schmid, F.X. (2009), Prot. Sci., 19, 6-18.

"The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fols but is devoid of catalytic activity."

49. Weininger, U., Jakob, R.P., Eckert, B., Schweimer, K., Schmid, F.X., Balbach, J. (2009), PNAS, 106, 12335-12340.

"A remote prolyl isomerization controls domain assembly via a hydrogen bonding network."

48. Weininger, U., Zeeb, M., Neumann, P., Stubbs, M.T., Lipps, G., Balbach, J. (2009), Biochemistry, 48, 10030-10037.

"Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus."

47. Schulenburg, C., Löw, C., Weininger, U., Mrestani-Klaus, C., hofmann, H., Balbach, J., Ulbrich-Hofmann, R., Arnold, U. (2009), Biochemistry, 48, 8449-8457.

"The folding pathway of onconase is directed by a conserved intermediate."

46. Pornsuriyasaka, P., Vetterb, C., Kaeothipa, S., Kovermann, M., Balbach, J., Steinborn, T., Demchenko, A.V. (2009), Chem. Commun., 42, 6370-6381.

"Coordination chemistry approach to the long-standing challenge of sthttp://www.physik.uni-halle.de/Fachgruppen/bio/cms_publ/group_publ.htmlereocontrolled chemical glycosylation."

45. Weininger U., Haupt C., Schweimer K., Graubner W., Kovermann M., Brüser T., Scholz C., Schaarschmidt P., Zoldak G., Schmid F.X., Balbach J. (2009), J. Mol. Biol., 387, 295-305.

"NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function."

44. Löw C., Homeyer N., Weininger U., Sticht H., Balbach J. (2009), ACS Chem. Biol., 4, 53-63.

"Conformational switch upon phosphorylation: human CDK inhibitor p19INK4d between the native and partially folded state."

43. Hofmann H., Weininger U., Löw C., Golbik R.P., Balbach J., Ulbrich-Hofmann R. (2009), J. Am. Chem. Soc., 131, 140-146.

"Fast amide proton exchange reveals close relation between native-state dynamics and unfolding kinetics."

42. Hoffmann A., Funkner A., Neumann P., Juhnke S., Walther M., Schierhorn A., Weininger U., Balbach J., Reuter G., Stubbs M.T. (2008), J. Biol. Chem., 47, 32598-32609.

"Biophysical Characterization of Refolded Drosophila Spatzle, a Cystine Knot Protein, Reveals Distinct Properties of Three Isoforms."

41. Löw C., Weininger U., Lee H., Schweimer K., Neundorf I., Beck-Sickinger A.G., Pastor R.W., Balbach J. (2008), Biophys. J., 95, 4315-4323.

"Structure and dynamics of Helix-0 of the N-BAR domain in Lipid Micelles and Bilayers."

40. Rohrberg J., Sachs R., Lodderstedt G., Sackewitz M., Balbach J., Schwarz E. (2008), FEBS Lett, 582, 1587-1592.

"Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR."

39. Löw C., Weininger U., Neumann P., Klepsch M., Lilie H., Stubbs M.T., Balbach J. (2008), PNAS, 105, 3779-3784.

"Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein."

38. Bosse-Doenecke E., Weininger U., Gopalswamy M., Balbach J., Knudsen S.M., Rudolph R. (2008), Protein Expr. Purif.,55, 114-121.

"High yield production of recombinant native and modified peptides exemplified by ligands for G-protein coupled receptors."

37. Lodderstedt G., Sachs R., Faust J., Bordusa F., Kühn U., Golbik R., Kerth A., Wahle E., Balbach J., Schwarz E. (2008), Biochemstry, 47, 2181-2189.

"Hofmeister Salts and Potential Therapeutic Compounds Accelerate in Vitro Fibril Formation of the N-Terminal Domain of PABPN1 Containing a Disease-Causing Alanine Extension."

36. Löw C., Weininger U., Zeeb M., Zhang W., Laue E.D., Schmid F.X., Balbach J. (2007), J. Mol. Biol., 373, 219-231.

"Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor p19(INK4d)."

35. Max, K.E., Zeeb, M. Bienert, R., Balbach, J., Heinemann, U. (2007), FEBS J., 274, 1265-1279.  

"Common mode of DNA binding to cold shock domains."

34. Zeeb, M., Max, K.E., Weininger, U., Löw, C., Sticht, H., Balbach, J. (2006), Nucleic Acids Res., 34, 4561-4571.  

"Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution."

33. Max, K.E., Zeeb, M., Bienert, R., Balbach, J., Heinemann, U. (2006), J. Mol. Biol., 360, 702-714.

"T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB."

32. Kliemannel, M., Weininger, U., Balbach, J., Schwarz, E., Rudolph, R. (2006), Biochemistry, 45, 3517-3524.

"Examination of the Slow Unfolding of Pro-Nerve Growth Factor Argues against a Loop Threading Mechanism for Nerve Growth Factor."

31. Scholz, C., Eckert, B., Hagn, F., Schaarschmidt, P., Balbach, J., Schmid, F.X. (2006), Biochemistry, 45, 20-33.

"SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities."

30. Szyperski, T., Mills, J.L., Perl, D., Balbach, J. (2005), Eur. Biophys. J., 21, 1-4.

"Combined NMR-observation of cold denaturation in supercooled water and heat denauration enables accurate measuerement of DeltaC(p) of protein unfolding."

29. Zeeb, M., Balbach, J. (2005), J. Am. Chem. Soc., 127, 13207-13212.

"NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements."

28. Hofweber, R., Horn, G. Langmann, T., Balbach, J., Kremer, W., Schmitz, G., Kalbitzer, H.R. (2005), FEBS J., 272, 4691-4702.

"The influence of cold shock proteins of transcription and translation studied in cell-free model systems."

27. Eckert, B., Martin, A., Balbach, L., Schmid, F.X. (2005), Nat. Struct. Mol. Biol., 12, 619-623.

"Prolyl isomerization as a molecular timer in phage infection."

26. Scholz, C., Schaarschmidt, P., Engel, A.M., Andres, H., Schmitt, U., Faatz, E., Balbach, J., Schmid, F.X. (2005), J. Mol. Biol. , 345, 1229-1241.

"Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules."

25. Kliemannel, M., Rattenholl, A., Golbik, R., Balbach, J., Lilie, H., Rudolph, R., Schwarz, E. (2004). FEBS Lett.,566, 207-212.

"The mature part of proNGF induces the structure of its pro-peptide."

24. Bienert, R., Zeeb, M., Dostal, L., Feske, A., Magg, C., Max, K., Welfle, H., Balbach, J., Heinemann, U. (2004), Acta Crystallogr D Biol Crystallogr, 60, 755-757.

"Single-stranded DNA bound to bacterial cold-shock proteins: preliminary crystallographic and Raman analysis."

23. Zeeb, M., Lipps, G., Lilie, H., Balbach, J. (2004), J. Mol. Biol. , 336, 227-240.

"Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus."

22. Zeeb, M., Jacob, M.H., Schindler, T., M., Balbach, J. (2003), J. Biomol. NMR , 27, 221-34.

"15N relaxation study of the cold shock protein CspB at various solvent viscosities."

21. Zeeb, M., Balbach, J. (2003), Protein Science, 12, 112-123.

"Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization."

20. Zeeb, M., Rösner, H.,  Zeslawski, W., Canet, D., Holak, T.A., Balbach, J. (2001), J. Mol. Biol., 315, 447-457.

"Protein folding and stability of human CDK inhibitor p19(INK4d)."

19. Steegborn, C., Schneider-Hassloff, H., Zeeb, M., Balbach, J. (2000), Biochemistry, 39, 7910-7919.

"Cooperativity of a protein folding reaction probed at multiple chain positions by real-time NMR spectroscopy."

18. Balbach, J., (2000), J. Am. Chem. Soc., 122, 5887-5888.

"Compaction during protein folding studied by real-time NMR diffusion experiments."

17. Forge, V., Wijesingha, R., Balbach, J., Brew, K., Robinson, C.V., Redfield, C., Dobson, C.M. (1999), J. Mol. Biol., 288, 673-688.

"Rapid collapse and slow structural reorganisation during the refolding of bovine a-lactalbumin."

16. Balbach, J., Steegborn, C., Schindler, T., Schmid, F.X. (1999), J. Mol. Biol. , 285, 829-842.

"A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy."

15. Balbach, J., Seip, S., Kessler, H., Scharf, M., Noushin Kaschani-Poor, N., Engels, J.W. (1998), Proteins: Struct. Funct. Genet.,33, 285-294.

"Structure and dynamic properties of the single disulfide-deficient a-Amylase Inhibi-tor [C45A/C73A]Tendamistat: An NMR study."

14. Balbach, J., Forge, V., Lau, W.S., Jones, J.A., van Nuland, N.A.J., Dobson, C.M. (1997) Proc. Natl. Acad. Sci. USA, 94, 7182-7185.

"Detection of residue contacts in a folding intermediate."

13. Jacob, M., Schindler, T., Balbach, J., Schmid, F.X. (1997) Proc. Natl. Acad. Sci. USA , 94, 5622-5627.

"Diffusion control in an elementary protein folding reaction."

12. van Nuland, N.A.J, Lau, W.S., Balbach, J., Forge, V., Dobson, C.M. (1996) Prog. Biophy. Mol. Biol., 65, 417.

"New NMR approaches for studying protein folding."

11. Balbach, J., Forge, V., Lau, W.S., van Nuland, N.A.J., Brew, K., Dobson, C.M. (1996) Science, 274, 1161-1163.

"Protein folding monitored at individual residues during a 2D NMR experiment."

10. Balbach, J., Forge, V., van Nuland, N.A.J., Winder, S.L., Hore, P.J., Dobson, C.M. (1995) Nature Struc. Biol., 2, 865-870.

"Following protein folding in real time using NMR spectroscopy."

9. Balbach, J., Kessler, H. (1994) J. Magn. Reson. , B 105, 83-87.

"13C-Edited double-quantum spectroscopy of peptides and proteins"

8. Seip, S., Balbach, J., Behrens, S., Kessler, H., Flükiger, K., de Meyer, R., Erni, B. (1994) Biochemistry, 33, 7174-7183.

"Mannose transporter of Escherichia coli. Backbone assignments and secondary structure of the IIA domain of the IIABMan subunit."

7. Markovic-Housley, Z., Balbach, J., Stolz, B., Génovésio-Taverne, J.-C. (1994), FEBS Lett., 340, 202-206.

"Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli."

6. Seip, S., Balbach, J., Kessler, H. (1994) J. Magn. Reson. , B 104, 172-179.

"Determination of backbone conformation of isotopically enriched proteins based on coupling constants."

5. Seip, S., Balbach, J., Kessler, H. (1993) J. Biomol. NMR , 3, 233-237.

"A simple way for sequential assignment in isotopically enriched proteins using a H(N)CACO correlation."

4. Kessler, H., Balbach, J., Müller, G., Mierke, D.F., Schmieder, P., Seip, S. (1993) J. Cell. Bioch. , S17C SIC, 207 und 246.

"New heteronuclear NMR Techniques for the determination of structures and Dynamics of peptides and proteins - consequences for drug design"

3. Seip, S., Balbach, J., Kessler, H. (1992) Angew. Chem. Int. Ed.Engl., 31, 1609-1611.

"Determination of the HN-Ha coupling constant in large isotopically enriched proteins."

2. Seip, S., Balbach, J., Kessler, H. (1992) J. Magn. Reson. , 100, 406-410.

"An improved technique for correlating backbone amide protons with 15N and Ha protons (HN(CA)H) in isotopically enriched proteins."

1. Mronga, S., Balbach, J. (1992) J. Magn. Reson., 98, 421-427.

"Multiplet structure in real cosine fourier-transformed zero-quantum spectra without axial peaks."

 

Übersichtsartikel:

3. Zeeb, M., Balbach, J. (2005), Prot. Pept. Lett. , 12, 139-146.

‘Millisecond protein folding studied by NMR spectroscopy.’

2. Zeeb, M., Balbach, J. (2004), Methods, 34, 65-74.

‘Protein folding studied by real-time NMR spectroscopy.’

1. van Nuland, N.A.J, Balbach, J., Forge, V., Dobson, C.M. (1998), Acc. Chem. Res., 31, 773-780.

‘Real-time NMR studies of protein folding.’

 

Buchbeiträge:

3. Zeeb, M., Balbach, J. (2004), in: ‘Handbook of protein folding I’ (J. Buchner, T. Kiefhaber, eds.), 536-572, Wiley-VCH, Weinheim.

‘Kinetic protein folding studies using NMR spectroscopy.’

2. Zeeb, M., Balbach, J. (2001), Nova Acta Leopoldina, Supp. 16, 57-58.

‘DNA binding and micro-viscosity effects on the folding of CspB . ’

1. Balbach, J., Schmid, F.X. (2000) in "Mechanisms of protein folding" (R.H. Pain, ed.), Oxford University Press.

"Proline isomerization and its catalysis in protein folding."


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