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The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate

Autor: W.J.H. van Berkel, E. Steensma, W.M.A.M. van Dongen, F. Vergeldt, C.P.M. van Mierlo

Publikováno v: Scopus-Elsevier
Protein Science, 7, 2331-2344
Protein Science 7 (1998)

A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins. The guanidinium hydrochloride induced unfolding of apoflavodoxin is demonstrated to be reversible. Apoflavodoxin thus can f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::944ebbb9c3162a5a0c990872039d3e27
http://www.scopus.com/inward/record.url?eid=2-s2.0-0031792027&partnerID=MN8TOARS

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