M
Marta A. S. Perez
Researcher at École Polytechnique Fédérale de Lausanne
Publications - 20
Citations - 418
Marta A. S. Perez is an academic researcher from École Polytechnique Fédérale de Lausanne. The author has contributed to research in topics: Alanine scanning & Protease. The author has an hindex of 11, co-authored 20 publications receiving 360 citations. Previous affiliations of Marta A. S. Perez include University of Porto.
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Journal ArticleDOI
Infrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG)
A. Masson,Michael K. Kamrath,Marta A. S. Perez,Matthew S. Glover,Ursula Rothlisberger,David E. Clemmer,Thomas R. Rizzo +6 more
TL;DR: Ion mobility and spectroscopic data combined with density functional theory (DFT) based molecular dynamics simulations confirm the presence of one major conformer per family, which arises from cis/trans isomerization about the proline residue.
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Computational Alanine Scanning Mutagenesis: MM-PBSA vs TI.
Silvia A. Martins,Marta A. S. Perez,Irina S. Moreira,Sérgio F. Sousa,Maria J. Ramos,Pedro A. Fernandes +5 more
TL;DR: This ASM protocol is a strong and efficient alternative to the systematic evaluation of protein-protein interfaces, involving hundreds of amino acid residues in search of hot-spots, at a fraction of the computational time required to run TI.
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The Structure of the Protonated Serine Octamer
Valeriu Scutelnic,Marta A. S. Perez,Mateusz Marianski,Stephan Warnke,Aurelien Gregor,Ursula Rothlisberger,Michael T. Bowers,Carsten Baldauf,Gert von Helden,Thomas R. Rizzo,Jongcheol Seo +10 more
TL;DR: The three-dimensional structure of Ser8H+ is determined by a combination of infrared spectroscopy and ab initio molecular dynamics simulations and explains both the homochiral preference and the experimentally observed facile replacement of two serine units.
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Accuracy of Density Functionals in the Prediction of Electronic Proton Affinities of Amino Acid Side Chains.
TL;DR: This work has analyzed how well DFT functionals describe the zero-point-exclusive proton affinity at 0 K, PAel0K, for the ionizable side chains of lysine (Lys), histidine (His), arginine (Arg), and aspartate (Asp–) as well as the cysteine (Cys–), serine (Ser–), and tyrosine (Tyr–) anions.
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Establishing the Catalytic Mechanism of Human Pancreatic α-Amylase with QM/MM Methods
Gaspar Pinto,Gaspar Pinto,Natércia F. Brás,Marta A. S. Perez,Pedro A. Fernandes,Nino Russo,Maria J. Ramos,Marirosa Toscano +7 more
TL;DR: The catalytic mechanism of human pancreatic α-amylase was determined with atomic detail using computational methods and it was shown that the rate limiting step was glycosylation, and its activation energy was in agreement with experimental values obtained for HPA.