CHARMM: The biomolecular simulation program
An overview of the CHARMM program as it exists today is provided with an emphasis on developments since the publication of the original CHARMM article in 1983.
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
- C. Bartels, T. Xia, M. Billeter, P. Güntert, K. Wüthrich
- ChemistryJournal of Biomolecular NMR
- 1 July 1995
XEASY was developed for work with 2D, 3D and 4D NMR data sets to provide maximal computer support for the analysis of spectra, while providing the user with complete control over the final resonance assignments.
Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model.
The free energy difference between "correctly" folded and misfolded secondary structures are of interest for understanding the alpha to beta transition that is thought to play a role in amyloid fibril formation.
GARANT‐a general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra
A new program for automatic resonance assignment of nuclear magnetic resonance (NMR) spectra of proteins, GARANT (General Algorithm for Resonance AssignmeNT), is introduced. Three principal elements…
Fast algorithm for peptide sequencing by mass spectroscopy.
- C. Bartels
- PhysicsBiomedical & environmental mass spectrometry
- 1 June 1990
An automatic algorithm for sequencing polypeptides from fast atom bombardment tandem mass spectra is presented.Based on graph theory considerations it finds the most probable sequences, even if the…
RAPD analysis of genetic variation between a group of rose cultivars and selected wild rose species
It is concluded that cultivated roses display a high level of genetic variability despite the fact that single morphological and physiological characters may be less polymorphic within rose groups, which contrasts with the widely accepted opinion of a lack of Genetic variability in roses.
Automated sequence-specific NMR assignment of homologous proteins using the program GARANT
The potential of GARANT for the assignment of homologous proteins when either the three-dimensional structure or the chemical shifts of the parent protein are known is demonstrated.
Size and physical map of the Campylobacter jejuni chromosome.
- P. Nuijten, C. Bartels, N. Bleumink-Pluym, W. Gaastra, B. V. D. van der Zeijst
- BiologyNucleic Acids Research
- 21 November 1990
The chromosome of Campylobacter jejuni was determined by field inversion gel electrophoresis of restriction endonuclease fragments using lambda DNA concatamers and yeast chromosomes to calibrate the size of the fragments.
Multidimensional adaptive umbrella sampling: Applications to main chain and side chain peptide conformations
The high efficiency of the technique renders multidimensional adaptive umbrella sampling possible and thereby enables uniform sampling of the conformational space spanned by several degrees of freedom and helps to calculate dynamical variables that are of interest.