i.e., DNA or RNA molecules and transmitted via transcription and translation processes. The understanding of biomolecular structure, function, dynamics and transport is a fundamental issue in molecular biology and biophysics. A traditional dogma is that sequence determines structure, while structure determines function [@Anfinsen:1973]. This, however, has been undermined by the fact that many intrinsically disordered proteins can also be functional [@Onuchic:1997; @White:1999; @Schroder:2005; @Chiti:2006]. Disordered proteins are associated with sporadic neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s disease and mad cow disease [@Chiti:2006; @Uversky:2008]. Randomness in disordered proteins is a consequence of protein flexibility, which is an intrinsic protein function. In general, the understanding of protein structure-function relationship is also crucial for shedding light on protein specification, protein-protein interactions, protein-drug binding that are essential to drug design and discovery, and improving human health and wellbeing.

Much of the present understanding of biomolecular structures and functions and their relationship come from experimental data that are collected from a number of means, such as macromolecular X-ray crystallography, nuclear magnetic resonance (NMR), cryo-electron microscopy (cryo-EM), electron paramagnetic resonance (EPR), multiangle light scattering, confocal laser-scanning microscopy, scanning capacitance microscopy, small angle scattering, ultra fast laser spectroscopy, etc. The major players for single macromolecules are X-ray 