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B H Jonsson

Showing results (31-40 of 70) with videos related to

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Biochemistry|April 29, 1997
Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase IIP Jonasson, G Aronsson, U Carlsson, et al.
FEBS Letters|February 5, 1998
Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase IIP Hammarström, B Kalman, B H Jonsson, et al.
Psychosomatic Medicine|June 13, 1998
Gastrin, cholecystokinin, and somatostatin in a laboratory experiment of patients with functional dyspepsiaB H Jonsson, K Uvnäs-Moberg, T Theorell, et al.
FEBS Letters|July 14, 1997
Remarkably slow folding of a small proteinG Aronsson, A C Brorsson, L Sahlman, et al.
European Journal of Biochemistry|March 15, 1997
The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeaeL C Chirică, B Elleby, B H Jonsson, et al.
Biochemistry|April 15, 1997
Formation of local native-like tertiary structures in the slow refolding reaction of human carbonic anhydrase II as monitored by circular dichroism on tryptophan mutantsD Andersson, P O Freskgård, B H Jonsson, et al.
Biochemistry|February 21, 1995
Folding and stability of the N-terminus of human carbonic anhydrase IIG Aronsson, L G Mårtensson, U Carlsson, et al.
European Journal of Biochemistry|February 1, 1993
Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase IIZ Liang, Y Xue, G Behravan, et al.
FEBS Letters|December 2, 1996
Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzymeB Sjöblom, B Elleby, K Wallgren, et al.
FEBS Letters|September 2, 1991
Folding around the C-terminus of human carbonic anhydrase II. Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineeringP O Freskgård, U Carlsson, L G Mårtensson, et al.
Pageof 7

Showing results (31-40 of 70) with videos related to

Sort By:
Pageof 7
Biochemistry|April 29, 1997
Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase IIP Jonasson, G Aronsson, U Carlsson, et al.
FEBS Letters|February 5, 1998
Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase IIP Hammarström, B Kalman, B H Jonsson, et al.
Psychosomatic Medicine|June 13, 1998
Gastrin, cholecystokinin, and somatostatin in a laboratory experiment of patients with functional dyspepsiaB H Jonsson, K Uvnäs-Moberg, T Theorell, et al.
FEBS Letters|July 14, 1997
Remarkably slow folding of a small proteinG Aronsson, A C Brorsson, L Sahlman, et al.
European Journal of Biochemistry|March 15, 1997
The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeaeL C Chirică, B Elleby, B H Jonsson, et al.
Biochemistry|April 15, 1997
Formation of local native-like tertiary structures in the slow refolding reaction of human carbonic anhydrase II as monitored by circular dichroism on tryptophan mutantsD Andersson, P O Freskgård, B H Jonsson, et al.
Biochemistry|February 21, 1995
Folding and stability of the N-terminus of human carbonic anhydrase IIG Aronsson, L G Mårtensson, U Carlsson, et al.
European Journal of Biochemistry|February 1, 1993
Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase IIZ Liang, Y Xue, G Behravan, et al.
FEBS Letters|December 2, 1996
Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzymeB Sjöblom, B Elleby, K Wallgren, et al.
FEBS Letters|September 2, 1991
Folding around the C-terminus of human carbonic anhydrase II. Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineeringP O Freskgård, U Carlsson, L G Mårtensson, et al.
Pageof 7