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Andrew P. Capaldi
Researcher at University of Arizona
Publications - 31
Citations - 2014
Andrew P. Capaldi is an academic researcher from University of Arizona. The author has contributed to research in topics: Protein folding & Phi value analysis. The author has an hindex of 18, co-authored 29 publications receiving 1791 citations. Previous affiliations of Andrew P. Capaldi include Howard Hughes Medical Institute & University of Leeds.
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Journal ArticleDOI
Orthogonal SARS-CoV-2 Serological Assays Enable Surveillance of Low-Prevalence Communities and Reveal Durable Humoral Immunity.
Tyler J. Ripperger,Jennifer L. Uhrlaub,Makiko Watanabe,Rachel O.L. Wong,Rachel O.L. Wong,Yvonne Castaneda,Hannah A. Pizzato,Hannah A. Pizzato,Mallory R. Thompson,Christine M. Bradshaw,Craig Weinkauf,Christian Bime,Heidi Erickson,Kenneth S. Knox,Billie Bixby,Sairam Parthasarathy,Sachin Chaudhary,Bhupinder Natt,Elaine Cristan,Tammer El Aini,Franz Rischard,Janet Campion,Madhav Chopra,Michael Insel,Afshin Sam,James Knepler,Andrew P. Capaldi,Catherine M. Spier,Michael D. Dake,Taylor Edwards,Matthew E. Kaplan,Serena Jain Scott,Cameron Hypes,Jarrod Mosier,David T. Harris,Bonnie LaFleur,Ryan Sprissler,Janko Nikolich-Žugich,Deepta Bhattacharya +38 more
TL;DR: It is concluded that neutralizing antibodies are stably produced for at least 5-7 months after SARS-CoV-2 infection.
Journal ArticleDOI
Im7 folding mechanism: misfolding on a path to the native state.
TL;DR: The results of this study support a hierarchical mechanism of protein folding and explain why the misfolding of Im7 occurs, and demonstrate that non-native interactions can play a significant role in folding, even for small proteins with simple topologies.
Journal ArticleDOI
Structure and function of a transcriptional network activated by the MAPK Hog1.
TL;DR: A quantitative model of the Hog1 MAPK-dependent osmotic stress response in budding yeast reveals that the Hog 1 and general stress pathways interact, at both the signaling and promoter level, to integrate information and create a context-dependent response.
Journal ArticleDOI
Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9.
TL;DR: The results show that the population of an intermediate in the refolding of the immunity protein structure is defined by the precise amino acid sequence rather than the global stability of the protein.
Journal ArticleDOI
Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate
Andrew P. Capaldi,M. C. Ramachandra Shastry,Colin Kleanthous,Heinrich Roder,Sheena E. Radford +4 more
TL;DR: Quantitative kinetic modeling of folding and unfolding data acquired over a wide range of urea concentrations demonstrate that this intermediate ensemble lies on a direct path from the unfolded to the native state.