Jonasson P - Search Results

1

Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonance.

Lindgren M, Svensson M, Freskgård PO, Carlsson U, Jonasson P, Mårtensson LG, Jonsson BH. Lindgren M, et al. Among authors: jonasson p. Biophys J. 1995 Jul;69(1):202-13. doi: 10.1016/S0006-3495(95)79892-7. Biophys J. 1995. PMID: 7669898 Free PMC article.

2

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase.

Fransson C, Freskgård PO, Herbertsson H, Johansson A, Jonasson P, Mårtensson LG, Svensson M, Jonsson BH, Carlsson U. Fransson C, et al. Among authors: jonasson p. FEBS Lett. 1992 Jan 13;296(1):90-4. doi: 10.1016/0014-5793(92)80410-i. FEBS Lett. 1992. PMID: 1730298 Free article.

3

Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues.

Svensson M, Jonasson P, Freskgård PO, Jonsson BH, Lindgren M, Mårtensson LG, Gentile M, Borén K, Carlsson U. Svensson M, et al. Among authors: jonasson p. Biochemistry. 1995 Jul 11;34(27):8606-20. doi: 10.1021/bi00027a010. Biochemistry. 1995. PMID: 7612602

4

Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II.

Mårtensson LG, Jonasson P, Freskgård PO, Svensson M, Carlsson U, Jonsson BH. Mårtensson LG, et al. Among authors: jonasson p. Biochemistry. 1995 Jan 24;34(3):1011-21. doi: 10.1021/bi00003a036. Biochemistry. 1995. PMID: 7827017

5

Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

Freskgård PO, Mårtensson LG, Jonasson P, Jonsson BH, Carlsson U. Freskgård PO, et al. Among authors: jonasson p. Biochemistry. 1994 Nov 29;33(47):14281-8. doi: 10.1021/bi00251a041. Biochemistry. 1994. PMID: 7947839

6

Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II.

Jonasson P, Aronsson G, Carlsson U, Jonsson BH. Jonasson P, et al. Biochemistry. 1997 Apr 29;36(17):5142-8. doi: 10.1021/bi961882a. Biochemistry. 1997. PMID: 9136875

Intrinsic tryptophan fluorescence was used to monitor the refolding in the 2 ms-60 s time range, and kinetic traces showing the contributions from each particular tryptophan were obtained by calculation of differences between the wild-type protein and the variants. Earlier assign …

Intrinsic tryptophan fluorescence was used to monitor the refolding in the 2 ms-60 s time range, and kinetic traces showing the contribution …

7

Structural and functional differences between carbonic anhydrase isoenzymes I and II as studied by site-directed mutagenesis.

Behravan G, Jonasson P, Jonsson BH, Lindskog S. Behravan G, et al. Among authors: jonasson p. Eur J Biochem. 1991 Jun 15;198(3):589-92. doi: 10.1111/j.1432-1033.1991.tb16054.x. Eur J Biochem. 1991. PMID: 1904817 Free article.

8

Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.

Jonasson P, Kjellsson A, Sethson I, Jonsson BH. Jonasson P, et al. FEBS Lett. 1999 Feb 26;445(2-3):361-5. doi: 10.1016/s0014-5793(99)00042-3. FEBS Lett. 1999. PMID: 10094490 Free article.

9

Affinity-assisted in vivo folding of a secreted human peptide hormone in Escherichia coli.

Samuelsson E, Jonasson P, Viklund F, Nilsson B, Uhlén M. Samuelsson E, et al. Among authors: jonasson p. Nat Biotechnol. 1996 Jun;14(6):751-5. doi: 10.1038/nbt0696-751. Nat Biotechnol. 1996. PMID: 9630984

10

The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study.

Kraulis PJ, Jonasson P, Nygren PA, Uhlén M, Jendeberg L, Nilsson B, Kördel J. Kraulis PJ, et al. Among authors: jonasson p. FEBS Lett. 1996 Jan 8;378(2):190-4. doi: 10.1016/0014-5793(95)01452-7. FEBS Lett. 1996. PMID: 8549831 Free article.

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