Ana Carolina de Mattos Zeri
NMR Facility Coordinator
Education Platform Coordinator
ana.zeri at lnbio.cnpem.br
Phone: +55 19 3512.1119
My personal research interests are in the areas of development and application of biophysical methods to the biosciences, and science education in non-formal environments.
At LNBio my research group employs Nuclear Magnetic Resonance Spectroscopy (NMR) to study biological samples, with applications in cancer research, bacterial growth machinery, and pathogen defense mechanisms. The NMR techniques we use allows us to determine the shape, at atomic level, of molecules such as proteins, and to investigate minute differences in the composition of biofluids, such as saliva, blood plasma and urine, and also of extracts from cells and leaves.
I am also interested in developing activities for small kids and teenagers, exposing them to basic biology and biotechnology laboratory tools, while providing activities mixing Portuguese and English (MicroGlobalScope link) language, in a non-formal context. With Dr Tiago Sobreira, I am working on a project with children from low-income communities, who attend an after-school program at a Campinas NGO (AAQQ), and are being trained as monitors for the activities with other kids. This is a partnership with Science House Foundation, aiming at inspiring a sense of wonder that can lead to a higher interest in science and learning.
We operate two high field NMR spectrometers dedicated to biological NMR experiments, mainly protein structure and protein-partner interaction studies, and also metabolic profiling. The NMR facility is an open laboratory, and the staff provides training and help with experiment setup and data analysis. We are always happy to hear from potential users, collaborators and students. Proposals can be submitted via our Users Services Portal.
More information here
- Ana Carolina M. Zeri – Researcher and Facility Coordinator
- Silvana Rocco – Researcher
- Maurício Luís Sforça – Assistant Researcher
Cancer cells Drug Metabolism in Leukemia investigated by NMR – Nuclear Magnetic Resonance, statistical methods and bioinformatics are employed in the investigation of the mechanisms of chemotherapy resistance in leukemia cell lines, and bone marrow transplant rejection in patients. – Cancer Biology Scientific Program –
- Rafael Canevarolo – PhD student (Unicamp)
- Marcos Alborghetti – PostDoctoral Fellow (FAPESP 2011/06441-3 )
- Dr. José Andres Yunes – Collaborator (Centro Infantil Boldrini)
Bacterial Cell Division – Structural bio-NMR is combined with genetics tools in a collaborative project aimed at an understanding of the bacterial cell division apparatus in B. subtilis. – Plants and Microorganisms Scientific Program –
- Frederico Gueiros Filho (IQ-USP) – collaborator (FAPESP 2010/51866-0)
- Patricia Castellen – PostDoctoral fellow (FAPESP 2010/51870-7 )
- Maria Luiza Caldas Nogueira – PhD student (Unicamp)
LNBio.educa and Training
We have opportunities for students and post-doctoral fellows.
LNBio at AAQQ and Pontos de Ciência – in a partnership with Science House Foundation (SHF), we assembled a small science laboratory at the headquarters of the NGO Associação Anhumas Quero-quero (AAQQ), in Campinas, to develop science based activities with kids from 6 to 18 years old, in a non-formal education context.
This project is a collaboration between LNBio and Science House Foundation, via a MicroGlobalScope grant, and part of their Pontos de Ciência initiative, which aims to bring science education and environment awareness to kids everywhere.
2003- 2006 – HHMI Post-doctoral fellow, Biophysics. Studies of translation under force using optical tweezers.
University of California, Berkeley/ Howard Hughes Medical Institute, Lewis Hall, Berkeley, CA . Advisors: Prof. Carlos Bustamante, Prof. Ignacio Tinoco Jr and Prof Harry Noller (UCSC)
2000 – 2003 – PhD in Chemistry and Biochemistry – University of California, San Diego, CA. Solid-state NMR studies of the major coat protein of the bacteriophage fd Advisor: Prof. Stanley J Opella
1997- 2000 – M.S. degree in Chemistry – University of Pennsylvania, Philadelphia, PA. Solid-state NMR studies of the major coat protein of the bacteriophage fd. Advisor: Prof. Stanley J. Opella
1995 – 1997 – M.S. degree in Physics – Universidade de São Paulo – Instituto de Fisica de São Carlos. Solid-state NMR analysis of seeds. Advisors: Dr. Tito Bonagamba (USP- São Carlos) and Dr. Luis A. Colnago (EMBRAPA – CNPDIA, São Carlos , SP)
1991 – 1994 – B.S. degree in Physics – Universidade de São Paulo – Instituto de Fisica de São Carlos
April 2005 – present
Facility Coordinator and Principal Investigator – NMR multiuser laboratory – LNBio/CNPEM
Rosselli-Murai LK, Sforça ML, Sassonia RC, Azzoni AR, Murai MJ, de Souza AP, Zeri AC. Structural characterization of the H-NS protein from Xylella fastidiosa and its interaction with DNA. Arch Biochem Biophys. 2012 Oct 1;526(1):22-8. Epub 2012 Jul 5. PubMed PMID: 22772065.
DF Oliveira, VAC Campos, ART Machado, WRJ Silva, ACM Zeri, VP Campos. Influence of volatile organic substances on the reproduction of Meloidogyne incognita in soybean and cotton plants. Nematologia Brasileira 2012, 35 (3/4), 55-62
Santos CR, Paiva JH, Sforça ML, Neves JL, Navarro RZ, Cota J, Akao PK, Hoffmam ZB, Meza AN, Smetana JH, Nogueira ML, Polikarpov I, Xavier-Neto J, Squina FM, Ward RJ, Ruller R, Zeri AC, Murakami MT. Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168. Biochem J. 2012 Jan 1;441(1):95-104. PubMed PMID: 21880019.
Murakami MT, Sforça ML, Neves JL, Paiva JH, Domingues MN, Pereira AL, Zeri AC, Benedetti CE. The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction. Proteins. 2010 Dec;78(16):3386-95. doi: 10.1002/prot.22846. Epub 2010 Sep 16. PubMed PMID: 20848643.
de Oliveira JF, Sforça ML, Blumenschein TM, Goldfeder MB, Guimarães BG, Oliveira CC, Zanchin NI, Zeri AC. Structure, dynamics, and RNA interaction analysis of the human SBDS protein. J Mol Biol. 2010 Mar 5;396(4):1053-69. Epub 2010 Jan 4. PubMed PMID: 20053358.
de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. Biochimie. 2009 Apr;91(4):475-83. Epub 2008 Dec 16. PubMed PMID: 19121363.
Opella SJ, Zeri AC, Park SH. Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy. Annu Rev Phys Chem. 2008;59:635-57. Review. PubMed PMID: 18393681.
Wen JD, Lancaster L, Hodges C, Zeri AC, Yoshimura SH, Noller HF, Bustamante C, Tinoco I. Following translation by single ribosomes one codon at a time. Nature. 2008 Apr 3;452(7187):598-603. Epub 2008 Mar 9. PubMed PMID: 18327250; PubMed Central PMCID: PMC2556548.
Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ. Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63. Epub 2003 May 15. Erratum in: Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):2024. PubMed PMID: 12750469; PubMed Central PMCID: PMC164468.
Veglia G, Zeri AC, Ma C, Opella SJ. Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins. Biophys J. 2002 Apr;82(4):2176-83. PubMed PMID: 11916873; PubMed Central PMCID: PMC1302011.
Lin K, Crocker JC, Zeri AC, Yodh AG. Colloidal interactions in suspensions of rods. Phys Rev Lett. 2001 Aug 20;87(8):088301. Epub 2001 Aug 1. Erratum in: Phys Rev Lett 2001 Dec 24;87(26):269902-1. PubMed PMID: 11497987.
Rosay M, Zeri AC, Astrof NS, Opella SJ, Herzfeld J, Griffin RG. Sensitivity-enhanced NMR of biological solids: dynamic nuclear polarization of Y21M fd bacteriophage and purple membrane. J Am Chem Soc. 2001 Feb 7;123(5):1010-1. PubMed PMID: 11456650.
Tan WM, Gu Z, Zeri AC, Opella SJ. Solid-state NMR triple-resonance backbone assignments in a protein. J Biomol NMR. 1999 Apr;13(4):337-42. PubMed PMID: 10353195.