NMR protein conformers described by network parameters: a preliminary study.

Abstract

NMR spectroscopy is one of the techniques of choice for the determination of protein structures. Its use has a number of positive aspects, among which the possibility to observe the influence of the solvent on the molecular structure, as well as the local movement of small molecular domains.However, due to the intrinsic flexibility of protein tertiary structures in solution, the NMR information does not lead to a single structure but to a set of conformers. Using the topological representation of such conformers we analyzed the corresponding network parameters, to enlight their association with some specific molecular feature. In this frame we showed that: i) the node degree parameter positively correlates with molecular ’compactness’, ii) the average shortest path length parameter positively correlates with molecular flexibility, and iii) as expected, the two parameters are anticorrelated between each other.