J
Javier Ruiz-Sanz
Researcher at University of Granada
Publications - 28
Citations - 721
Javier Ruiz-Sanz is an academic researcher from University of Granada. The author has contributed to research in topics: Circular dichroism & SH3 domain. The author has an hindex of 18, co-authored 25 publications receiving 675 citations. Previous affiliations of Javier Ruiz-Sanz include University of Cambridge & Spanish National Research Council.
Papers
More filters
Journal ArticleDOI
Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.
TL;DR: The growing polypeptide chain has little tendency to form stable structure until it is largely synthesized, and what structures are formed are nonnative and lack, in particular, the native secondary structural elements of alpha-helix and beta-sheet.
Journal ArticleDOI
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
TL;DR: The nucleation site of folding of CI2 does not accumulate in the starting state for the folding reaction, but remains embryonic until there are sufficient long range interactions to stabilize it.
Journal ArticleDOI
Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway.
Javier Ruiz-Sanz,Jose Luis Neira,Fernando J. Corrales,Daniel E. Otzen,Andreas G. Ladurner,Alan R. Fersht +5 more
TL;DR: An extensive biophysical characterization of ten fragments using different conformational probes is presented, finding structures that develop as the polypeptide chain increases in length parallel the structural features present in the nucleus for the folding of intact protein, which develops in the transition state.
Journal ArticleDOI
The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase
Anne-Marie Lambeir,Jan Backmann,Javier Ruiz-Sanz,Vladimir V. Filimonov,Jens Erik Nielsen,Inari Kursula,B.V. Norledge,Rik K. Wierenga +7 more
TL;DR: Study of a stable monomersic triose phosphate isomerase variant confirmed that the phenomenon persists in the monomer, and the guanidinium chloride dependence of the unfolding constant was smaller than expected from studies involving monomeric model proteins.
Journal ArticleDOI
Protein fragments as models for events in protein folding pathways: protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2).
TL;DR: There is a good correlation between the changes on mutation of thefree energy of association of fragments and the changes in free energy of folding of the uncleaved parent protein, and the rate constants for association correlate well with the rate constant of refolding of the respective uncleaved proteins.