Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement

Autor: Carlo P. M. van Mierlo, Adrie H. Westphal, Bregje J. de Kort, Sanne M. Nabuurs

Publikováno v: European Biophysics Journal
European Biophysics Journal with Biophysics Letters, 39, 4, pp. 689-98
European Biophysics Journal, 39(4), 689-698
European Biophysics Journal 39 (2010) 4
European Biophysics Journal with Biophysics Letters, 39, 689-98

Item does not contain fulltext Transient structures in unfolded proteins are important in elucidating the molecular details of initiation of protein folding. Recently, native and non-native secondary structure have been discovered in unfolded A. vine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81aa5379db4244803467365f5218a690
https://hdl.handle.net/2066/89810

The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates

Autor: Carlo P. M. van Mierlo, Monique B. Kamphuis, Yves J. M. Bollen

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America 103 (2006) 11
Proceedings of the National Academy of Sciences of the United States of America, 103(11), 4095-4100
Proceedings of the National Academy of Sciences of the United States of America, 103, 4095-4100. National Acad Sciences
Bollen, Y J M, Kamphuis, M B & Van Mierlo, C P M 2006, ' The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates. ', Proceedings of the National Academy of Sciences of the United States of America, vol. 103, pp. 4095-4100 . https://doi.org/10.1073/pnas.0509133103

Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and NMR spectroscopy. Knowledge about these metastable states is required to better understand the onset of folding-related d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0179b28241d433ec79d8be1472d4abf2
https://doi.org/10.1073/pnas.0509133103

Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein

Autor: Jan Willem Borst, Carlo P. M. van Mierlo, Adrie H. Westphal, Simon Lindhoud

Publikováno v: PLoS ONE
PLoS ONE, Vol 7, Iss 9, p e45746 (2012)
PLoS ONE 7 (2012) 9
PLoS ONE, 7(9)

Partially folded protein species transiently form during folding of most proteins. Often, these species are molten globules, which may be on- or off-pathway to the native state. Molten globules are ensembles of interconverting protein conformers that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db3a61ab6084afce0017ec098ba47f87
https://pubmed.ncbi.nlm.nih.gov/23029219

Distant residues mediate picomolar binding affinity of a protein cofactor

Autor: Adrie H. Westphal, Simon Lindhoud, Yves J. M. Bollen, Willem J. H. van Berkel, Carlo P. M. van Mierlo

Publikováno v: Bollen, Y J M, Westphal, A H, Lindhoud, S, van Berkel, W J & van Mierlo, C P 2012, ' Distant residues mediate picomolar binding affinity of a protein cofactor ', Nature Communications, vol. 3, pp. 1010 . https://doi.org/10.1038/ncomms2010
Nature Communications, 3. Nature Publishing Group
Nature Communications, 3
Nature Communications
Nature Communications 3 (2012)

Numerous proteins require cofactors to be active. Computer simulations suggest that cooperative interaction networks achieve optimal cofactor binding. There is a need for the experimental identification of the residues crucial for stabilizing these n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b006a952b9c195ab7217da007d30311
https://research.vu.nl/en/publications/d5d8c1ec-2196-449d-8ae0-e46928cfde07

Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding

Autor: Daphne H. E. W. Huberts, Simon Lindhoud, Adrie H. Westphal, Ruchira Engel, Sanne M. Nabuurs, Antonie J. W. G. Visser, Carlo P. M. van Mierlo

Publikováno v: Journal of Biological Chemistry, 283(41), 27383-27394
Engel, R, Westphal, A H, Huberts, D H E W, Nabuurs, S M, Lindhoud, S, Visser, A J W G & Van Mierlo, C P M 2008, ' Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin unfolding. ', Journal of Biological Chemistry, vol. 283, pp. 27383-27394 . https://doi.org/10.1074/jbc.M802393200
Journal of Biological Chemistry 283 (2008) 41
Journal of Biological Chemistry, 283, 27383-27394. American Society for Biochemistry and Molecular Biology Inc.

To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding. Here, the influence of crowding on in vitro apoflavodoxin folding, which involves a relatively stable off-pathway inter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03481588dd6ea896e1f28e1070ba93f6
https://research.wur.nl/en/publications/macromolecular-crowding-compacts-unfolded-apoflavodoxin-and-cause