#Indeed iscribe md series#

Using the high-resolution NMR structure of the CA C-terminal domain (CTD) dimer and in particular the unique interface identified, it was possible to reconstruct a model for a tubular assembly of CA protein that fit extremely well into the cryoEM density map. Previous structural analysis of two- and three-dimensional arrays provided a molecular model of the capsid protein (CA) hexamer and revealed three interfaces in the lattice. In mature HIV-1 particles a conical-shaped capsid core encloses the viral RNA genome. This entails a derailment of the normal host defense pathways, rendering HIV resistant to cell-mediated destruction responses. Once HIV gets inside the cell, it takes over the cellular machinery, turning it into a factory for its own reproduction. HIV and other retroviruses use a Trojan horse style of infection, taking advantage of a cloak that shields its genome till the time is ripe to open the shield. GronenbronÂ â 'Synergy between NMR, cryo-EM and large-scale MD simulations - An all atom model of a native HIV capsid' Date: Monday, April 3rdÂ 2017, 3pm, GBSF 1005. All who knew him will miss his kind and cheerful humor, his smile and his generous spirit. He was born in Albany, NY, on April 18th, 1937.ĭavid Weaver possessed an easy manner, a sense of fairness, curiosity and an enjoyment of life that was evident in his teaching and relations with colleagues.

A Fellow of the American Physical Society, Dr Weaver also served as the chair of the Tufts Department of Physics and Astronomy from 1989 to 2002. He held degrees in Chemistry from Rensselaer Polytechnic Institute and in Physical Chemistry from Iowa State University. He was a regular visitor at labs overseas and in the United States, and he authored or co-authored a number of significant scientific publications. Karplus and other collaborators to improve his understanding of important biophysical problems. Weaver received grants from NASA, NATO, Bruker Optics, and the NIH to establish computer facilities at Tufts where he continued to work with students, Dr. The field has been completely transformed in recent years because of its assumed importance for understanding the large number of protein sequences available from genome projects, says Karplus, and because of the realization that misfolding can lead to a wide range of human diseases.ĭr. But by the mid-1990s experimental studies had shown that the model did indeed describe the folding mechanism of many proteins. The Diffusion-Collision Model was ahead of its time because the data needed to test it were not available when it was published in 1976. Martin Karplus at Harvard during a sabbatical in 1972, and they began a collaboration that culminated in a paper about a then theoretical diffusion-collision model for protein folding (Nature, 1976). At the University of Rome, Italy, as a visiting CNN Fellow at the Frascati National Laboratory, he became more and more interested in applying his mathematical skills to gain a better understanding of molecular dynamics. Weaver's interests continued to shift towards some of the key unsolved problems in biology. While he continued to make significant contributions in high-energy physics, for which he received tenure at Tufts in 1969, Dr. After spending a year and a half as a NATO Fellow at the European Center for Nuclear Research (CERN), in Geneva, Switzerland, he returned to Tufts and began to think about how he could apply his physics background to problems in biology.

Weaver focused his early research on high-energy physics, studying photon production and elementary particles. He was impressed with the research and faculty at the UC Davis Genome Center, where he was planning to spend his sabbatical year 2006â∲007.ĭr. Weaver made significant contributions to the understanding of protein folding. Weaver, a prominent biophysics researcher and professor at Tufts University.ĭr.

#Indeed iscribe md series#

Weaver Endowed Lecture Series in Biophysics and Computational Biology is dedicated to the memory of David L.