J. Backmann

发表

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures

L. Wyns, J. Martial, D. Maes, 1999, Proteins.

Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.

G Vriend, G. Vriend, G. Neubauer, 1999, Protein engineering.

Intricate Interactions within the ccd Plasmid Addiction System*

Lode Wyns, Joris Messens, Remy Loris, 2002, The Journal of Biological Chemistry.

The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.

J. Nielsen, R. Wierenga, V. Filimonov, 2000, European journal of biochemistry.

Thermally induced hydrogen exchange processes in small proteins as seen by FTIR spectroscopy

D. Naumann, U. Hahn, H. Fabian, 1996, Proteins.

THE THERMALLY INDUCED HYDROGEN EXCHANGE IN DIFFERENT PROTEINS AS SEEN BY FTIR SPECTROSCOPY

D. Naumann, H. Fabian, J. Backmann, 1995 .

Biophysical and Structural Properties of DNA·diC14-amidine Complexes

D. Maes, J. Ruysschaert, J. Backmann, 2000, The Journal of Biological Chemistry.

Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.

D. Naumann, H. Fabian, J. Backmann, 1996, Biochemistry.

Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy.

D. Naumann, H. Mantsch, U. Hahn, 1994, Biochemistry.

The structural differences between bovine lens αA‐ and αB‐crystallin

J. Backmann, T. Aerts, J. Clauwaert, 2000 .

Hydrogen Peroxide-induced Structural Alterations of RNase A*

P. Lasch, D. Naumann, O. Ullrich, 2001, The Journal of Biological Chemistry.

Analysis of a water mediated protein-protein interactions within RNase T1.

J. Steyaert, R. Loris, J. Backmann, 2000, Biochemistry.

A correlation between thermal stability and structural features of staphylokinase and selected mutants: a Fourier-transform infrared study.

J. Backmann, W. Hübner, B. Schlott, 1996, Biochimica et biophysica acta.

Defossilization of pharmaceutical manufacturing

Kristi L. Budzinski, J. Backmann, Lea Wollensack, 2021, Current Opinion in Green and Sustainable Chemistry.

The thermodynamic stability of the proteins of the ccd plasmid addiction system.

L. Wyns, J. Backmann, J. Messens, 2000, Journal of molecular biology.

[28] Thermodynamic analysis of hyperthermostable oligomeric proteins

J. Backmann, G. Schäfer, Jan Backmann, 2001 .

Hydrophobic core manipulations in ribonuclease T1.

J. Steyaert, R. Loris, M. Prévost, 2001, Biochemistry.

Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius.

L. Wyns, J. Backmann, G. Schäfer, 1998, Journal of molecular biology.

Thermodynamic analysis of hyperthermostable oligomeric proteins.

J. Backmann, G. Schäfer, J Backmann, 2001, Methods in enzymology.

Temperature‐jump‐induced refolding of ribonuclease A: A time‐resolved FTIR spectroscopic study

D. Naumann, H. Fabian, J. Backmann, 1995, FEBS letters.

X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1.

U. Hahn, W. Saenger, C. Kisker, 1994, European journal of biochemistry.

Analysis of a water mediated protein-protein interactions within RNase T1.

J. Steyaert, R. Loris, J. Backmann, 2000, Biochemistry.