Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugation
(2013) In Journal of Peptide Science 19(5). p.283-292- Abstract
- alpha-Helical coiled coil structures, which are noncovalently associated heptad repeat peptide sequences, are ubiquitous in nature. Similar amphipathic repeat sequences have also been found in helix-containing proteins and have played a central role in de novo design of proteins. In addition, they are promising tools for the construction of nanomaterials. Small-angle X-ray scattering (SAXS) has emerged as a new biophysical technique for elucidation of protein topology. Here, we describe a systematic study of the self-assembly of a small ensemble of coiled coil sequences using SAXS and analytical ultracentrifugation (AUC), which was correlated with molecular dynamics simulations. Our results show that even minor sequence changes have an... (More)
- alpha-Helical coiled coil structures, which are noncovalently associated heptad repeat peptide sequences, are ubiquitous in nature. Similar amphipathic repeat sequences have also been found in helix-containing proteins and have played a central role in de novo design of proteins. In addition, they are promising tools for the construction of nanomaterials. Small-angle X-ray scattering (SAXS) has emerged as a new biophysical technique for elucidation of protein topology. Here, we describe a systematic study of the self-assembly of a small ensemble of coiled coil sequences using SAXS and analytical ultracentrifugation (AUC), which was correlated with molecular dynamics simulations. Our results show that even minor sequence changes have an effect on the folding topology and the self-assembly and that these differences can be observed by a combination of AUC, SAXS, and circular dichroism spectroscopy. A small difference in these methods was observed, as SAXS for one peptide and revealed the presence of a population of longer aggregates, which was not observed by AUC. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3843487
- author
- Malik, Leila ; Nygaard, Jesper LU ; Christensen, Niels J. ; Streicher, Werner W. ; Thulstrup, Peter W. ; Arleth, Lise and Jensen, Knud J.
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- coiled coil, SAXS, AUC, MD
- in
- Journal of Peptide Science
- volume
- 19
- issue
- 5
- pages
- 283 - 292
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000317932900004
- scopus:84876413091
- pmid:23505212
- ISSN
- 1099-1387
- DOI
- 10.1002/psc.2497
- language
- English
- LU publication?
- yes
- id
- dee0c4e7-1852-4019-abd8-fcc846247fca (old id 3843487)
- date added to LUP
- 2016-04-01 10:37:28
- date last changed
- 2022-01-26 00:56:31
@article{dee0c4e7-1852-4019-abd8-fcc846247fca,
abstract = {{alpha-Helical coiled coil structures, which are noncovalently associated heptad repeat peptide sequences, are ubiquitous in nature. Similar amphipathic repeat sequences have also been found in helix-containing proteins and have played a central role in de novo design of proteins. In addition, they are promising tools for the construction of nanomaterials. Small-angle X-ray scattering (SAXS) has emerged as a new biophysical technique for elucidation of protein topology. Here, we describe a systematic study of the self-assembly of a small ensemble of coiled coil sequences using SAXS and analytical ultracentrifugation (AUC), which was correlated with molecular dynamics simulations. Our results show that even minor sequence changes have an effect on the folding topology and the self-assembly and that these differences can be observed by a combination of AUC, SAXS, and circular dichroism spectroscopy. A small difference in these methods was observed, as SAXS for one peptide and revealed the presence of a population of longer aggregates, which was not observed by AUC. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.}},
author = {{Malik, Leila and Nygaard, Jesper and Christensen, Niels J. and Streicher, Werner W. and Thulstrup, Peter W. and Arleth, Lise and Jensen, Knud J.}},
issn = {{1099-1387}},
keywords = {{coiled coil; SAXS; AUC; MD}},
language = {{eng}},
number = {{5}},
pages = {{283--292}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Peptide Science}},
title = {{Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugation}},
url = {{http://dx.doi.org/10.1002/psc.2497}},
doi = {{10.1002/psc.2497}},
volume = {{19}},
year = {{2013}},
}