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Your search keyword '"Hammarstrom, Per"' showing total 3 results
Start Over Author "Hammarstrom, Per" Topic protein folding -- research
3 results on '"Hammarstrom, Per"'

1. Conformational rearrangements of tail-less complex polypeptide 1 (TCP-1) ring complex (TRiC)-bound actin

Author

Villebeck, Laila, Persson, Malin, Shi-Lu Luan, Hammarstrom, Per, Lindgren, Mikael, and Jonsson, Bengt-Harald

Subjects
Polypeptides -- Properties, Polypeptides -- Structure, Protein folding -- Research, Actin -- Properties, Actin -- Structure, Biological sciences, Chemistry
Abstract

A natural eukaryotic chaperonin system [tail-less complex polypeptide 1 (TCP-1) ring complex (TRiC) and its target protein actin] is examined to determine if the active participation of the chaperonin in the folding process is evolutionary-conserved. The results have shown that TRiC has an active role in rearranging the bound actin molecule.

Published
2007

2. Thermodynamic interrogation of a folding disease, mutant mapping of position 107 in human carbonic anhydrase II linked to marble brain disease

Author

Almstedt, Karin, Martensson, Lars-Goran, Carlsson, Uno, and Hammarstrom, Per

Subjects
Mutation (Biology) -- Research, Protein folding -- Research, Thermodynamics -- Research, Biological sciences, Chemistry
Abstract

The thermodynamics of destabilizing effects of the H107Y mutation, in human carbonic anhydrase II linked to marble brain disease (MBD) is demonstrated. The results suggest that the mutation is caused by long-range sterical destabilizing effects of the bulky tyrosine residue.

Published
2008

3. Activity, folding, misfolding, and aggregation in vitro of the naturally occurring human tissue factor mutant R200W

Author

Wirehn, Jimmy, Carlsson, Karin, Herland, Anna, Persson, Egon, Carlsson, Uno, Svensson, Magdalena, and Hammarstrom, Per

Subjects
Coagulation -- Research, Protein folding -- Research, Protein research, Biological sciences, Chemistry
Abstract

A study reports the activity, folding, and aggregation behavior of the R200W mutant of the 219-residue soluble extracellular domain of tissue factor [(sub s)TF(sub R200W)] compared to that of the wild-type protein [(sub s)TF(sub wt)]. The study concludes that the lowered activity for FX activation and the propensity of the mutant protein to misfold and aggregate, both would contribute to decreased coagulation activity in TF(sub R200W) carriers.

Published
2005

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