Profiles

Jose Farias-Rico

Jose Farias

Postdoc

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Works at Department of Biochemistry and Biophysics
Telephone 08-674 76 56
Email jose.farias@dbb.su.se
Visiting address Svante Arrhenius väg 16
Room A 431
Postal address Institutionen för biokemi och biofysik 106 91 Stockholm

About me

Proteins are the nano-machines that support life on earth. They perform nearly every function in the cell, encompassing processes from DNA replication to neuronal communication. During my PhD training I studied how nature evolves proteins to create the vast diversity of shapes and functions that we observe today. Later, it became obvious that understanding the process of folding (or how proteins assume their shape) is crucial to describe the relationship structure-function in proteins.  While the protein-folding problem is somewhat well understood outside of the cell in the test tube, this is not enough to fully explain how these biomolecules fold—and misfold causing human disease—under relevant biological conditions. Currently, I am working on protein folding in the ribosome in the laboratory from Gunnar von Heijne. 

 

Research

Research group: Gunnar von Heijne

Publications

A selection from Stockholm University publication database
  • 2018. Jose Arcadio Farias-Rico (et al.). Proceedings of the National Academy of Sciences of the United States of America 115 (40), e9280-E9287

    During the last five decades, studies of protein folding in dilute buffer solutions have produced a rich picture of this complex process. In the cell, however, proteins can start to fold while still attached to the ribosome (cotranslational folding) and it is not yet clear how the ribosome affects the folding of protein domains of different sizes, thermodynamic stabilities, and net charges. Here, by using arrest peptides as force sensors and on-ribosome pulse proteolysis, we provide a comprehensive picture of how the distance from the peptidyl transferase center in the ribosome at which proteins fold correlates with protein size. Moreover, an analysis of a large collection of mutants of the Escherichia coli ribosomal protein 56 shows that the force exerted on the nascent chain by protein folding varies linearly with the thermodynamic stability of the folded state, and that the ribosome environment disfavors folding of domains of high net-negative charge.

  • 2017. José Arcadio Farías-Rico (et al.). FEBS Letters 591 (1), 155-163

    Recent work has demonstrated that cotranslational folding of proteins or protein domains in, or in the immediate vicinity of, the ribosome exit tunnel generates a pulling force on the nascent polypeptide chain that can be detected using a so-called translational arrest peptide (AP) engineered into the nascent chain as a force sensor. Here, we show that AP-based force measurements combined with systematic Ala and Trp scans of a zinc-finger domain that folds in the exit tunnel can be used to identify the residues that are critical for intraribosomal folding. Our results suggest a general approach to characterize the folded state(s) that may form as a protein domain moves progressively down the ribosome exit tunnel.

Show all publications by Jose Farias at Stockholm University

Last updated: November 14, 2018

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