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Journal of Molecular Biology|February 10, 1995
High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE dataN A van Nuland, R Boelens, R M Scheek, et al.Biophysical Chemistry|November 1, 1991
Conformation and aggregation of M13 coat protein studied by molecular dynamicsJ C Sanders, N A van Nuland, O Edholm, et al.Journal of Biomolecular NMR|August 23, 2012
Structure from NMR and molecular dynamics: Distance restraining inhibits motion in the essential subspaceR M Scheek, N A van Nuland, B L de Groot, et al.European Journal of Biochemistry|December 15, 1992
Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopyN A van Nuland, J Grötzinger, K Dijkstra, et al.Journal of Molecular Biology|October 29, 1998
Slow folding of muscle acylphosphatase in the absence of intermediatesN A van Nuland, F Chiti, N Taddei, et al.The Journal of Biological Chemistry|July 10, 1999
Development of enzymatic activity during protein folding. Detection of a spectroscopically silent native-like intermediate of muscle acylphosphataseF Chiti, N Taddei, E Giannoni, et al.Proteins|November 1, 1996
An extended sampling of the configurational space of HPr from E. coliB L de Groot, A Amadei, R M Scheek, et al.Science (New York, N.Y.)|November 15, 1996
Protein folding monitored at individual residues during a two-dimensional NMR experimentJ Balbach, V Forge, W S Lau, et al.Biochemistry|March 7, 1998
Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pHF Chiti, N A van Nuland, N Taddei, et al.Nature Structural Biology|October 1, 1995
Following protein folding in real time using NMR spectroscopyJ Balbach, V Forge, N A van Nuland, et al.Pageof 2