Westphal AH - Search Results

1

Fluorescence of Alexa fluor dye tracks protein folding.

Lindhoud S, Westphal AH, Visser AJ, Borst JW, van Mierlo CP. Lindhoud S, et al. Among authors: westphal ah. PLoS One. 2012;7(10):e46838. doi: 10.1371/journal.pone.0046838. Epub 2012 Oct 8. PLoS One. 2012. PMID: 23056480 Free PMC article.

2

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

Engel R, Westphal AH, Huberts DHEW, Nabuurs SM, Lindhoud S, Visser AJWG, van Mierlo CPM. Engel R, et al. Among authors: westphal ah. J Biol Chem. 2008 Oct 10;283(41):27383-27394. doi: 10.1074/jbc.M802393200. Epub 2008 Jul 18. J Biol Chem. 2008. PMID: 18640986 Free article.

3

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

Visser NV, Westphal AH, van Hoek A, van Mierlo CP, Visser AJ, van Amerongen H. Visser NV, et al. Among authors: westphal ah. Biophys J. 2008 Sep;95(5):2462-9. doi: 10.1529/biophysj.108.132001. Biophys J. 2008. PMID: 18708472 Free PMC article.

4

Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules.

Nabuurs SM, Westphal AH, van Mierlo CP. Nabuurs SM, et al. Among authors: westphal ah. J Am Chem Soc. 2008 Dec 17;130(50):16914-20. doi: 10.1021/ja803841n. J Am Chem Soc. 2008. PMID: 19053416

5

Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.

Nabuurs SM, Westphal AH, van Mierlo CP. Nabuurs SM, et al. Among authors: westphal ah. J Am Chem Soc. 2009 Feb 25;131(7):2739-46. doi: 10.1021/ja8089476. J Am Chem Soc. 2009. PMID: 19170491

6

Topological switching between an alpha-beta parallel protein and a remarkably helical molten globule.

Nabuurs SM, Westphal AH, aan den Toorn M, Lindhoud S, van Mierlo CP. Nabuurs SM, et al. Among authors: westphal ah. J Am Chem Soc. 2009 Jun 17;131(23):8290-5. doi: 10.1021/ja9014309. J Am Chem Soc. 2009. PMID: 19456154

7

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

Nabuurs SM, de Kort BJ, Westphal AH, van Mierlo CP. Nabuurs SM, et al. Among authors: westphal ah. Eur Biophys J. 2010 Mar;39(4):689-98. doi: 10.1007/s00249-009-0556-4. Epub 2009 Nov 6. Eur Biophys J. 2010. PMID: 19894043 Free PMC article.

8

A general approach for detecting folding intermediates from steady-state and time-resolved fluorescence of single-tryptophan-containing proteins.

Laptenok SP, Visser NV, Engel R, Westphal AH, van Hoek A, van Mierlo CP, van Stokkum IH, van Amerongen H, Visser AJ. Laptenok SP, et al. Among authors: westphal ah. Biochemistry. 2011 May 3;50(17):3441-50. doi: 10.1021/bi101965d. Epub 2011 Apr 7. Biochemistry. 2011. PMID: 21425856

9

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

Lindhoud S, Westphal AH, Borst JW, van Mierlo CP. Lindhoud S, et al. Among authors: westphal ah. PLoS One. 2012;7(9):e45746. doi: 10.1371/journal.pone.0045746. Epub 2012 Sep 21. PLoS One. 2012. PMID: 23029219 Free PMC article.

10

Rise-time of FRET-acceptor fluorescence tracks protein folding.

Lindhoud S, Westphal AH, van Mierlo CP, Visser AJ, Borst JW. Lindhoud S, et al. Among authors: westphal ah. Int J Mol Sci. 2014 Dec 19;15(12):23836-50. doi: 10.3390/ijms151223836. Int J Mol Sci. 2014. PMID: 25535076 Free PMC article.

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