Dynamics of small, folded proteins

Petra Rovó, Dóra K. Menyhárd, Gábor Náray-Szabó, András Perczel

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Beyond static properties, like primary sequence, folding, electrostatics, etc. protein action is also influenced by dynamic factors, which may essentially influence structure and function. In this chapter first we give a short outline of various methods for the computer modelling of protein dynamics, then discuss the most important experimental technique, nuclear magnetic resonance spectroscopy applied to proteins. Combined application of these two methods will be illustrated on two small proteins, extensively studied in our laboratory. First we discuss the Trp-cage protein, to our knowledge the smallest one with essential attributes of basic protein properties. Our second case study deals with podocin, an interesting small protein. Its dynamic properties determine potential malfunction, the inheritance of a specific kidney disease.

Original languageEnglish
Title of host publicationProtein Modelling
PublisherSpringer International Publishing
Pages223-248
Number of pages26
Volume9783319099767
ISBN (Electronic)9783319099767
ISBN (Print)3319099752, 9783319099750
DOIs
Publication statusPublished - Jul 1 2014

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ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Rovó, P., Menyhárd, D. K., Náray-Szabó, G., & Perczel, A. (2014). Dynamics of small, folded proteins. In Protein Modelling (Vol. 9783319099767, pp. 223-248). Springer International Publishing. https://doi.org/10.1007/978-3-319-09976-7_10