Hammarström P - Search Results

1

High-resolution probing of local conformational changes in proteins by the use of multiple labeling: unfolding and self-assembly of human carbonic anhydrase II monitored by spin, fluorescent, and chemical reactivity probes.

Hammarström P, Owenius R, Mårtensson LG, Carlsson U, Lindgren M. Hammarström P, et al. Biophys J. 2001 Jun;80(6):2867-85. doi: 10.1016/S0006-3495(01)76253-4. Biophys J. 2001. PMID: 11371460 Free PMC article.

2

Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II.

Hammarström P, Kalman B, Jonsson BH, Carlsson U. Hammarström P, et al. FEBS Lett. 1997 Dec 22;420(1):63-8. doi: 10.1016/s0014-5793(97)01488-9. FEBS Lett. 1997. PMID: 9450551 Free article.

3

EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction.

Persson M, Hammarström P, Lindgren M, Jonsson BH, Svensson M, Carlsson U. Persson M, et al. Among authors: hammarstrom p. Biochemistry. 1999 Jan 5;38(1):432-41. doi: 10.1021/bi981442e. Biochemistry. 1999. PMID: 9890926

4

Structural mapping of an aggregation nucleation site in a molten globule intermediate.

Hammarström P, Persson M, Freskgârd PO, Mârtensson LG, Andersson D, Jonsson BH, Carlsson U. Hammarström P, et al. J Biol Chem. 1999 Nov 12;274(46):32897-903. doi: 10.1074/jbc.274.46.32897. J Biol Chem. 1999. PMID: 10551854 Free article.

5

Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity.

Hammarström P, Persson M, Owenius R, Lindgren M, Carlsson U. Hammarström P, et al. J Biol Chem. 2000 Jul 28;275(30):22832-8. doi: 10.1074/jbc.M000649200. J Biol Chem. 2000. PMID: 10811634 Free article.

6

Is the unfolded state the Rosetta Stone of the protein folding problem?

Hammarström P, Carlsson U. Hammarström P, et al. Biochem Biophys Res Commun. 2000 Sep 24;276(2):393-8. doi: 10.1006/bbrc.2000.3360. Biochem Biophys Res Commun. 2000. PMID: 11027486 Review.

7

Cofactor-induced refolding: refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II).

Andersson D, Hammarström P, Carlsson U. Andersson D, et al. Among authors: hammarstrom p. Biochemistry. 2001 Mar 6;40(9):2653-61. doi: 10.1021/bi000957e. Biochemistry. 2001. PMID: 11258876

8

Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL.

Hammarstrom P, Persson M, Carlsson U. Hammarstrom P, et al. J Biol Chem. 2001 Jun 15;276(24):21765-75. doi: 10.1074/jbc.M010858200. Epub 2001 Feb 26. J Biol Chem. 2001. PMID: 11278767 Free article.

Recently, we found that HCA II binding causes such an inflation of the GroEL molecule, and this probably represents the mechanism by which GroEL actively stretches its protein substrates apart (Hammarstrom, P., Persson, M., Owenius, R., Lindgren, M., and Carlsson, U …

Recently, we found that HCA II binding causes such an inflation of the GroEL molecule, and this probably represents the mechanism by which G …

9

Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II.

Persson M, Harbridge JR, Hammarström P, Mitri R, Mårtensson LG, Carlsson U, Eaton GR, Eaton SS. Persson M, et al. Among authors: hammarstrom p. Biophys J. 2001 Jun;80(6):2886-97. doi: 10.1016/S0006-3495(01)76254-6. Biophys J. 2001. PMID: 11371461 Free PMC article.

10

Phase memory relaxation times of spin labels in human carbonic anhydrase II: pulsed EPR to determine spin label location.

Huber M, Lindgren M, Hammarström P, Mårtensson LG, Carlsson U, Eaton GR, Eaton SS. Huber M, et al. Among authors: hammarstrom p. Biophys Chem. 2001 Dec 25;94(3):245-56. doi: 10.1016/s0301-4622(01)00239-3. Biophys Chem. 2001. PMID: 11804734

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