Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lise Nesgaard"'
Autor:
Pankaj Sehgal, Gunna Christiansen, Hidekazu Doe, Lise Nesgaard, Kell K. Andersen, Daniel E. Otzen, Jonas Høeg Hansen
Publikováno v:
Otzen, D, Nesgaard, L, Andersen, K, Hansen, J H, Christiansen, G, Doe, H & Seligal, P 2008, ' Aggregation of S6 in a quasi-native state by sub-micellar SDS ', Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1784, no. 2, pp. 400-414 . https://doi.org/10.1016/j.bbapap.2007.11.010
Anionic surfaces promote protein fibrillation in vitro and in vivo. Monomeric SDS has also been shown to stimulate this process. We describe the dynamics of conformational changes and aggregative properties of the model protein S6 at sub-micellar SDS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12494b43e657477c58fb9bfdb76af02e
https://doi.org/10.1016/j.bbapap.2007.11.010
https://doi.org/10.1016/j.bbapap.2007.11.010
Autor:
Shona Pedersen, Eduardo P. Melo, Lise Nesgaard, Daniel E. Otzen, Søren Risom Kristensen, Ricardo P. Baptista
Publikováno v:
Biopolymers. 83:619-629
We have studied the thermal stability of the triglyceride-hydrolyzing enzyme cutinase from F. solani pisi at pH values straddling the pI (pH 8.0). At the pI, increasing the protein concentration from 5 to 80 μM decreases the apparent melting tempera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16af4e173ff4cffbcc7ab73bba0a8716
https://doi.org/10.1002/bip.20598
https://doi.org/10.1002/bip.20598
Publikováno v:
Nesgaard, L W, Vad, B, Christiansen, G & Otzen, D 2009, ' Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan ', B B A-Molecular Cell Research, vol. 1794, pp. 84-93 .
Nesgaard, L, Vad, B, Christiansen, G & Otzen, D 2009, ' Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan ', Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1794, no. 1, pp. 84-93 . https://doi.org/10.1016/j.bbapap.2008.09.021
Nesgaard, L, Vad, B, Christiansen, G & Otzen, D 2009, ' Kinetic partitioning between aggregation and vesicle permeabilization by modified ADan ', Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1794, no. 1, pp. 84-93 . https://doi.org/10.1016/j.bbapap.2008.09.021
The neurodegenerative illness Familial Danish Dementia (FDD) is linked to formation and aggregation of the 34-residue ADan peptide, whose cytotoxicity may be mediated by membrane interactions. Here we characterize the derived peptide SerADan, in whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b46d66f318c9dfda9931ef32a5e1b3
https://pubmed.ncbi.nlm.nih.gov/18977466
https://pubmed.ncbi.nlm.nih.gov/18977466
Autor:
Lise Nesgaard, Daniel E. Otzen, Anders Malmendal, Søren Vrønning Hoffmann, Christian Beyschau Andersen
Publikováno v:
Nesgaard, L W, Hoffmann, S V, Andersen, C B, Malmendal, A & Otzen, D 2008, ' Characterization of Dry Globular Proteins and Protein Fibrils by Synchrotron Radiation Vacuum UV Circular Dichroism ', Biopolymers, vol. 89, no. 9, pp. 779-795 .
Nesgaard, L, Hoffmann, S V, Andersen, C B, Malmendal, A & Otzen, D 2008, ' Characterization of dry globular proteins and protein fibrils by synchrotron radiation vacuum UV circular dichroism ', Biopolymers, vol. 89, no. 9, pp. 779-795 . https://doi.org/10.1002/bip.21011
Aarhus University
Nesgaard, L, Hoffmann, S V, Andersen, C B, Malmendal, A & Otzen, D 2008, ' Characterization of dry globular proteins and protein fibrils by synchrotron radiation vacuum UV circular dichroism ', Biopolymers, vol. 89, no. 9, pp. 779-795 . https://doi.org/10.1002/bip.21011
Aarhus University
Circular dichroism using synchrotron radiation (SRCD) can extend the spectral range down to approximately 130 nm for dry proteins, potentially providing new structural information. Using a selection of dried model proteins, including alpha-helical, b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bca6b57d46000f4bcefd889d38491038
https://pure.au.dk/portal/da/publications/characterization-of-dry-globular-proteins-and-protein-fibrils-by-synchrotron-radiation-vacuum-uv-circular-dichroism(4dbddb50-a00d-11dd-889c-000ea68e967b).html
https://pure.au.dk/portal/da/publications/characterization-of-dry-globular-proteins-and-protein-fibrils-by-synchrotron-radiation-vacuum-uv-circular-dichroism(4dbddb50-a00d-11dd-889c-000ea68e967b).html
Publikováno v:
Otzen, D, Sehgal, P & Nesgaard, L 2007, ' Alternative membrane protein conformations in alcohols ', Biochemistry, vol. 46, no. 14, pp. 4348-4359 .
Alcohols modulate the oligomerization of membrane proteins in lipid bilayers. This can occur indirectly by redistributing lateral membrane pressure in a manner which correlates with alcohol hydrophobicity. Here we investigate the direct impact of dif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d8d95fc941fd13c58c33dc78019f606
https://pubmed.ncbi.nlm.nih.gov/17371052
https://pubmed.ncbi.nlm.nih.gov/17371052
Autor:
Brian S. Vad, Mads Davidsen, Reinhard Wimmer, Lise Nesgaard, Kell K. Andersen, Søren Mølgaard, Daniel E. Otzen, Hans Henrik Kristensen
Publikováno v:
Wimmer, R, Andersen, K, Davidsen, M, Mølgaard, S, Vad, B & Otzen, D 2006, ' Versatile interactions of the antimicrobial peptide Novispirin with detergents and lipids ', Biochemistry, vol. 45, no. 2, pp. 481-497 . https://doi.org/10.1021/bi051876r
Wimmer, R, Andersen, K, Davidsen, M, Mølgaard, S, Nesgaard, L, Kristensen, H H, Vad, B & Otzen, D 2006, ' Versatile interactions of the antimicrobial peptide novispirin with detergents and lipids ', Paper presented at 22nd International Conference on Magnetic Resonance in Biological Systems, Göttingen, Germany, 20/08/2006-26/08/2006 . < http://pubs.acs.org/doi/pdfplus/10.1021/bi051876r >
Wimmer, R, Andersen, K, Davidsen, M, Mølgaard, S, Nesgaard, L, Kristensen, H H, Vad, B & Otzen, D 2006, ' Versatile interactions of the antimicrobial peptide novispirin with detergents and lipids ', Paper presented at 22nd International Conference on Magnetic Resonance in Biological Systems, Göttingen, Germany, 20/08/2006-26/08/2006 . < http://pubs.acs.org/doi/pdfplus/10.1021/bi051876r >
Novispirin G-10 is an 18-residue designed cationic peptide derived from the N-terminal part of an antimicrobial peptide from sheep. This derivative is more specific for bacteria than the parent peptide. We have analyzed Novispirin's interactions with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d540eb6bd255c186197cfffe832ebd6b
https://vbn.aau.dk/da/publications/a2d5c9e0-b68f-11db-8b72-000ea68e967b
https://vbn.aau.dk/da/publications/a2d5c9e0-b68f-11db-8b72-000ea68e967b