Structure and dynamics of proteins by high-resolution NMR spectroscopy, SAXS, and computation

• Grant number: 13/50355-0
• Support Opportunities: Regular Research Grants
• Start date: October 01, 2013
• End date: September 30, 2014
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Agreement: Ohio State University
• Principal Investigator: Roberto Kopke Salinas
• Grantee: Roberto Kopke Salinas
• Principal researcher abroad: Mark Foster
• Institution abroad: Ohio State University, Columbus, United States
• Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil
• Associated research grant: 11/07777-5 - Cyclic di-GMP signaling and the Type IV macromolecule secretion system in Xanthomonas citri, AP.TEM

Abstract

The dynamic properties of many proteins are essential to their function, yet our understanding of protein dynamics, the time-dependent fluctuations in molecular structure, remain poorly understood. Protein dynamics play a role in critical cellular processes including metabolism, gene regulation and signal transduction. The proposed research plan aims to provide critical insights into the dynamic behavior of proteins through a combination of Nuclear Magnetic Resonance (NMR) spectroscopy, computational molecular dynamics simulations, and small angle X-ray scattering (SAXS). OSU and USP have complementary expertise and infrastructure for these studies, the proposed work will build upon existing collaboration, and will seed a new collaborative framework for studying the dynamics of proteins. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

ABIKO, LAYARA AKEMI; VITALE, PHELIPE M.; FAVARO, DENIZE C.; HAUK, PRICILA; LI, DA-WEI; YUAN, JIAQI; BRUSCHWEILER-LI, LEI; SALINAS, ROBERTO K.; BRUSCHWEILER, RAFAEL. Model for the allosteric regulation of the Na+/Ca2+ exchanger NCX. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v. 84, n. 5, p. 580-590, MAY 2016. (13/50355-0, 13/17883-2, 11/07777-5)