Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Santiago E. Faraj, Martín E. Noguera, José María Delfino, Javier Santos

ABSTRACT

Local events that affect specific regions of proteins are of utmost relevance for stability and function. The aim of this study is to quantitatively assess the importance of locally-focused dynamics by means of a simple chemical modification procedure. Taking human Frataxin as a working model, we investigated local fluctuations of the C-terminal region (the last 16 residues of the protein) by means of three L → C replacement mutants: L98C, L200C and L203C. The conformation and thermodynamic stability of each variant was assessed. All the variants exhibited native features and high stabilities: 9.1 (wild type), 8.1 (L198C), 7.0 (L200C) and 10.0 kcal mol-1 (L203C). In addition, kinetic rates of Cys chemical modification by DTNB and DTDPy were measured, conformational dynamics data were extracted and free energy for the local unfolding of the C-terminal region was estimated. The analysis of these results indicates that the conformation of the C-terminal region fluctuates with partial independence from global unfolding events. Additionally, numerical fittings of the kinetic model of the process suggest that the local transition occurs in the seconds to minutes timescale. In fact, standard free energy differences for local unfolding were found to be significantly lower than those of the global unfolding reaction, showing that chemical modification results may not be explained in terms of the global unfolding reaction alone. These results provide unequivocal experimental evidence of local phenomena with global effects and contribute to understanding how global and local stability are linked to protein dynamics. More... »

PAGES

1731

Journal

TITLE

Scientific Reports

ISSUE

1

VOLUME

9

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-019-39429-2

DOI

http://dx.doi.org/10.1038/s41598-019-39429-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112058689

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30742023


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