Zobrazeno 1 - 10 of 85 pro vyhledávání: '"C.P.M. van Mierlo"'
1
5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin
Autor: Jaap Broos, Antonie J. W. G. Visser, Adrie H. Westphal, C.P.M. van Mierlo, Nina V. Visser, Sanne M. Nabuurs, H. van Amerongen, A. van Hoek
Publikováno v: FEBS Letters 583 (2009) 17
FEBS Letters, 583(17), 2785-2788. Wiley
FEBS Letters, 583, 17, pp. 2785-8
FEBS Letters, 583(17), 2785-2788
FEBS Letters, 583, 2785-8
The apoflavodoxin protein from Azotobacter vinelandii harboring three tryptophan (Trp) residues, was biosynthetically labeled with 5-fluorotryptophan (5-FTrp). 5-FTrp has the advantage that chemical differences in its microenvironment can be sensitiv
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::718539f00f29616d116efbb059da5269
https://hdl.handle.net/2066/81703
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2
Refolding of Adsorbed Bovine α-Lactalbumin during Surfactant Induced Displacement from a Hydrophobic Interface
Autor: Maarten F. M. Engel, C.P.M. van Mierlo, Antonie J. W. G. Visser
Publikováno v: Langmuir, 19, 2929-2937. American Chemical Society
Langmuir, 19(7), 2929-2937
Engel, M F M, Visser, A J W G & van Mierlo, C P M 2003, ' Refolding of adsorbed bovine alpha-lactalbumin during surfactant induced displacement from a hydrophobic interface. ', Langmuir, vol. 19, pp. 2929-2937 . https://doi.org/10.1021/la026767h
Langmuir 19 (2003) 7
Little is known about the changes in protein conformation that occur after displacement of a protein from an interface. Here, results are presented that give insight into the conformation of bovine a-lactalbumin (BLA) molecules that are displaced fro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::711df07f3fd297d6017270a7b6d57921
https://doi.org/10.1021/la026767h
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3
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
Autor: E. Steensma, C.P.M. van Mierlo
Publikováno v: Journal of Biotechnology 79 (2000)
Journal of Biotechnology, 79, 281-298
In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introdu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef4a8c6a69f5a3079e83d9a1a35e5b02
https://doi.org/10.1016/s0168-1656(00)00244-3
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4
Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology 1 1Edited by P. E. Wright
Autor: E. Steensma, C.P.M. van Mierlo
Publikováno v: Journal of Molecular Biology. 282:653-666
The structural characteristics of Azotobacter vinelandii apoflavodoxin II have been determined using multidimensional NMR spectroscopy. Apoflavodoxin has a stable, well-ordered core but its flavin binding region is flexible. The local stability of ap
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7a9ee750a2e8363b6cb8c6b168db8cec
https://doi.org/10.1006/jmbi.1998.2045
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5
Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
Autor: W. van den Berg, E. Steensma, W.M.A.M. van Dongen, Yves J. M. Bollen, M.J.M. Nijman, P.A. de Jager, C.P.M. van Mierlo
Publikováno v: Protein Science. 7:306-317
As a first step to determine the folding pathway of a protein with an alpha/beta doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimension
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::742c4b7759de96e39f94f6b854583e58
https://doi.org/10.1002/pro.5560070210
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6
Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor
Autor: Thomas E. Creighton, Nigel J. Darby, G.H.E. Scott, David Neuhaus, C.P.M. van Mierlo
Publikováno v: Journal of Molecular Biology 224 (1992)
Journal of Molecular Biology, 224, 905-911
The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30–51), (30–51, 5–14), and (30–51, 5–38); these are important kinetic intermediates in folding, even th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d945a78b25de2e7d9312ac6b4d9eb06
https://doi.org/10.1016/0022-2836(92)90458-v
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7
'Noncooperative formation of the off-pathway molten globule during folding of the a-ß parallel protein apoflavodoxin'
Autor: Adrie H. Westphal, C.P.M. van Mierlo, Sanne M. Nabuurs
Publikováno v: Journal of the American Chemical Society, 131(7), 2739-2746
Journal of the American Chemical Society, 131, 2739-46
Journal of the American Chemical Society 131 (2009) 7
Journal of the American Chemical Society, 131, 7, pp. 2739-46
Item does not contain fulltext During folding of many proteins, molten globules are formed. These partially folded forms of proteins have a substantial amount of secondary structure but lack virtually all tertiary side-chain packing characteristic of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6be4cbc721388829902ced1e0d3656d
https://research.wur.nl/en/publications/noncooperative-formation-of-the-off-pathway-molten-globule-during
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8
The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor
Autor: Nigel J. Darby, C.P.M. van Mierlo, Thomas E. Creighton
Publikováno v: FEBS Letters 279 (1991) 1
FEBS Letters, 279(1), 61-64
An analogue of the BPTI folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation or the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8829b720d843bdb48ef60f70ca305654
https://doi.org/10.1016/0014-5793(91)80251-w
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9
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