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

Authors

  • Lisa Beatrice Caruso Sapienza - Univ. of Rome
  • Alessandro Giuliani Ist. Superiore di Sanità
  • Cesare Manetti Sapienza - Univ. of Rome
  • Alfredo Colosimo Sapienza Univ. of Rome

Keywords:

Protein NMR spectroscopy, Protein structural networks, Sperm Whale Myoglobin

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.

Author Biographies

Lisa Beatrice Caruso, Sapienza - Univ. of Rome

Dept. S.A.I.M.L.A.L.

Alessandro Giuliani, Ist. Superiore di Sanità

Dept. of Environment and Primary Prevention 

Cesare Manetti, Sapienza - Univ. of Rome

Dept. of Chemistry

Alfredo Colosimo, Sapienza Univ. of Rome

Dept. S.A.I.M.L.A.L.

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Published

30-12-2013

How to Cite

Caruso, L. B., Giuliani, A., Manetti, C., & Colosimo, A. (2013). NMR protein conformers described by network parameters: a preliminary study. Biophysics and Bioengineering Letters, 6. Retrieved from https://rosa.uniroma1.it/rosa00/index.php/biophysics_and_bioengineering/article/view/11435

Issue

Section

Section 1: Regular papers

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