Biomolecular simulations have become a method of choice in the
last decade to gain a detailed understanding of the structure and
dynamic properties of biomolecules. Classical molecular dynamic (MD)
simulations are able to sample timescales up to milliseconds on systems
composed of large biomolecules immersed in explicit water molecule
containing simulation boxes including necessary ions, ligands, etc.
required to simulate a realistic molecular system. Enhanced sampling
methods of MD simulations have the potential of further improving the
characterisation of the conformational space of biomolecules. Advanced
biomolecular force fields exists for protein, carbohydrates, nucleic
acids, such as the AMBER and CHARMM force fields that are continuously
being improved.
Nuclear Magnetic Resonance (NMR) Spectroscopy is a powerful technique that gives insight into the structure and interaction of molecules, but also
can be used as an analytical method.
In order to interpret the experimental data and gain further understanding, NMR can be combined with molecular mechanics based modelling calculations and structural bioinformatics.