Van Nuland NA - Search Results

1

A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding.

Reader JS, Van Nuland NA, Thompson GS, Ferguson SJ, Dobson CM, Radford SE. Reader JS, et al. Among authors: van nuland na. Protein Sci. 2001 Jun;10(6):1216-24. doi: 10.1110/ps.52801. Protein Sci. 2001. PMID: 11369860 Free PMC article.

2

Development of enzymatic activity during protein folding. Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase.

Chiti F, Taddei N, Giannoni E, van Nuland NA, Ramponi G, Dobson CM. Chiti F, et al. Among authors: van nuland na. J Biol Chem. 1999 Jul 16;274(29):20151-8. doi: 10.1074/jbc.274.29.20151. J Biol Chem. 1999. PMID: 10400629 Free article.

3

Following protein folding in real time using NMR spectroscopy.

Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM. Balbach J, et al. Among authors: van nuland na. Nat Struct Biol. 1995 Oct;2(10):865-70. doi: 10.1038/nsb1095-865. Nat Struct Biol. 1995. PMID: 7552710

4

Protein folding monitored at individual residues during a two-dimensional NMR experiment.

Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM. Balbach J, et al. Among authors: van nuland na. Science. 1996 Nov 15;274(5290):1161-3. doi: 10.1126/science.274.5290.1161. Science. 1996. PMID: 8895458

5

Detection of residue contacts in a protein folding intermediate.

Balbach J, Forge V, Lau WS, Jones JA, van Nuland NA, Dobson CM. Balbach J, et al. Among authors: van nuland na. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7182-5. doi: 10.1073/pnas.94.14.7182. Proc Natl Acad Sci U S A. 1997. PMID: 9207065 Free PMC article.

6

Characterization of folding the four-helix bundle protein Rop by real-time NMR.

van Nuland NA, Dobson CM, Regan L. van Nuland NA, et al. Protein Eng Des Sel. 2008 Mar;21(3):165-70. doi: 10.1093/protein/gzm081. Protein Eng Des Sel. 2008. PMID: 18299292

7

Slow cooperative folding of a small globular protein HPr.

Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM. Van Nuland NA, et al. Biochemistry. 1998 Jan 13;37(2):622-37. doi: 10.1021/bi9717946. Biochemistry. 1998. PMID: 9425085 Free article.

8

Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH.

Chiti F, van Nuland NA, Taddei N, Magherini F, Stefani M, Ramponi G, Dobson CM. Chiti F, et al. Among authors: van nuland na. Biochemistry. 1998 Feb 3;37(5):1447-55. doi: 10.1021/bi971692f. Biochemistry. 1998. PMID: 9477974

9

Slow folding of muscle acylphosphatase in the absence of intermediates.

van Nuland NA, Chiti F, Taddei N, Raugei G, Ramponi G, Dobson CM. van Nuland NA, et al. J Mol Biol. 1998 Nov 6;283(4):883-91. doi: 10.1006/jmbi.1998.2009. J Mol Biol. 1998. PMID: 9790846

10

Structural characterization of the transition state for folding of muscle acylphosphatase.

Chiti F, Taddei N, van Nuland NA, Magherini F, Stefani M, Ramponi G, Dobson CM. Chiti F, et al. Among authors: van nuland na. J Mol Biol. 1998 Nov 6;283(4):893-903. doi: 10.1006/jmbi.1998.2010. J Mol Biol. 1998. PMID: 9790847

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