Van Dael H - Search Results

1

Structural characterisation and comparison of the native and A-states of equine lysozyme.

Morozova-Roche LA, Arico-Muendel CC, Haynie DT, Emelyanenko VI, Van Dael H, Dobson CM. Morozova-Roche LA, et al. Among authors: van dael h. J Mol Biol. 1997 May 23;268(5):903-21. doi: 10.1006/jmbi.1997.0996. J Mol Biol. 1997. PMID: 9180380

2

An equilibrium partially folded state of human lysozyme at low pH.

Haezebrouck P, Joniau M, Van Dael H, Hooke SD, Woodruff ND, Dobson CM. Haezebrouck P, et al. Among authors: van dael h. J Mol Biol. 1995 Feb 24;246(3):382-7. doi: 10.1006/jmbi.1994.0093. J Mol Biol. 1995. PMID: 7877162

3

Partially folded states of equine lysozyme. Structural characterization and significance for protein folding.

Van Dael H, Haezebrouck P, Morozova L, Arico-Muendel C, Dobson CM. Van Dael H, et al. Biochemistry. 1993 Nov 9;32(44):11886-94. doi: 10.1021/bi00095a018. Biochemistry. 1993. PMID: 8218261

4

Structural basis of the stability of a lysozyme molten globule.

Morozova LA, Haynie DT, Arico-Muendel C, Van Dael H, Dobson CM. Morozova LA, et al. Among authors: van dael h. Nat Struct Biol. 1995 Oct;2(10):871-5. doi: 10.1038/nsb1095-871. Nat Struct Biol. 1995. PMID: 7552711

5

A Ca(2+)-binding chimera of human lysozyme and bovine alpha-lactalbumin that can form a molten globule.

Pardon E, Haezebrouck P, De Baetselier A, Hooke SD, Fancourt KT, Desmet J, Dobson CM, Van Dael H, Joniau M. Pardon E, et al. Among authors: van dael h. J Biol Chem. 1995 May 5;270(18):10514-24. doi: 10.1074/jbc.270.18.10514. J Biol Chem. 1995. PMID: 7737986 Free article.

6

Kinetic and equilibrium intermediate states are different in LYLA1, a chimera of lysozyme and alpha-lactalbumin.

Haezebrouck P, Noyelle K, Joniau M, Van Dael H. Haezebrouck P, et al. Among authors: van dael h. J Mol Biol. 1999 Oct 29;293(3):703-18. doi: 10.1006/jmbi.1999.3186. J Mol Biol. 1999. PMID: 10543961

7

The fast folding pathway in human lysozyme and its blockage by appropriate mutagenesis: a sequential stopped-flow fluorescence study.

Noyelle K, Joniau M, Van Dael H. Noyelle K, et al. Among authors: van dael h. J Mol Biol. 2001 May 11;308(4):807-19. doi: 10.1006/jmbi.2001.4620. J Mol Biol. 2001. PMID: 11350176

8

The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme.

Griko YV, Freire E, Privalov G, van Dael H, Privalov PL. Griko YV, et al. Among authors: van dael h. J Mol Biol. 1995 Sep 29;252(4):447-59. doi: 10.1006/jmbi.1995.0510. J Mol Biol. 1995. PMID: 7563064 Free article.

9

Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysis.

Polverino de Laureto P, Frare E, Gottardo R, Van Dael H, Fontana A. Polverino de Laureto P, et al. Among authors: van dael h. Protein Sci. 2002 Dec;11(12):2932-46. doi: 10.1110/ps.0205802. Protein Sci. 2002. PMID: 12441391 Free PMC article.

10

Equilibrium and kinetic studies on folding of canine milk lysozyme.

Van Dael H, Haezebrouck P, Joniau M. Van Dael H, et al. Protein Sci. 2003 Mar;12(3):609-19. doi: 10.1110/ps.0235303. Protein Sci. 2003. PMID: 12592031 Free PMC article.

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