Peter Damberg
Karolinska Institutet
47 Papers
414 Citations
Peter Damberg is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Medicine & Random coil. The author has an hindex of 21, co-authored 42 publications. Previous affiliations of Peter Damberg include Karolinska University Hospital & University of California, San Diego.
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Papers
Resident Neural Stem Cells Restrict Tissue Damage and Neuronal Loss After Spinal Cord Injury in Mice
Hanna Sabelström,Moa Stenudd,Pedro Réu,Pedro Réu,David O. Dias,Marta Elfineh,Sofia Zdunek,Peter Damberg,Christian Göritz,Jonas Frisén +9 more
TL;DR: It is shown that scarring by neural stem cell–derived astrocytes is required to restrict secondary enlargement of the lesion and further axonal loss after spinal cord injury and one distinct component of the glial scar, deriving from resident neural stem cells, is required for maintaining the integrity of the injured spinal cord.
292
Positioning of the Alzheimer Aβ(1–40) peptide in SDS micelles using NMR and paramagnetic probes
TL;DR: Comparison of experimentally determined translational diffusion coefficients for SDS and Aβ(1–40) show that the size of SDS micelle is not significantly changed by interaction with Aβ, and should be buried in the hydrophobic interior of the micelle.
156
Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1–40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length
TL;DR: The results from biophysical studies of Ab and fragments thereof, are presented in this paper, where the results from NMR diffusion measurements as well as the 3JHNH values show that increasing the temperature from 4 C to 15 C induces a structure transition from PII propensity to a beta strand propensity around 15 C and to a random coil conformation at higher temperature.
155
The Alzheimer β-peptide shows temperature-dependent transitions between left-handed 31-helix, β-strand and random coil secondary structures
TL;DR: In this article, temperature-induced structural transitions of the full length Alzheimer amyloid beta-peptide [A(beta)(1-40) peptide] and fragments of it were studied using CD and 1H NMR spectroscopy.
123
Structure and positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes
Jüri Jarvet,Jens Danielsson,Peter Damberg,Marta Oleszczuk,Astrid Gräslund +4 more
- 01 Jan 2007
TL;DR: The results from biophysical studies of Ab and fragments thereof, are presented in this paper, where the results from NMR diffusion measurements as well as the 3JHNH values show that increasing the temperature from 4 C to 15 C induces a structure transition from PII propensity to a beta strand propensity around 15 C and to a random coil conformation at higher temperature.
116