Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Timothy G. Connolly"'
Autor:
Michael E. Colvin, Yuhui Huang, Xingyuan Shen, Timothy G. Connolly, Jennifer Q. Lu, Changchun Wang
Publikováno v:
Macromolecular Rapid Communications. 37:1904-1911
A low-energy triggered switch that can generate mechanoresponse has great technological potential. A submolecular moiety, S-dibenzocyclooctadiene (DBCOD) that is composed of a flexible eight-membered ring connecting to a phenyl ring at each end, unde
Publikováno v:
Biophysical Journal. 110:644a
Proteins exist along a continuum from order to disorder, and many are now known to contain both folded and unfolded regions. Molecular dynamics (MD) simulations of intrinsically disordered proteins reveal deficiencies in most current analysis tools.
Autor:
Amanda Miguel, Michael E. Colvin, Robert L. Wang, Ajay Gopinathan, Joshua L. Phillips, Timothy G. Connolly, Shawn Newsam
Publikováno v:
Biophysical Journal. 106:610a-611a
Intrinsically disordered proteins (IDPs) exist in a naturally unfolded state consisting of a vast ensemble of transient conformations. Molecular dynamics (MD) simulations of IDPs are capable of estimating subsets of these ensembles, but most current
Autor:
Michael E. Colvin, Joshua L. Phillips, Edmond Y. Lau, Robert L. Wang, Timothy G. Connolly, Amanda Miguel
Publikováno v:
Biophysical Journal. 104:233a-234a
The nuclear pore complex (NPC) is a massive protein structure located on the nuclear envelope serving as a selective gateway between the cellular cytoplasm and nucleoplasm. The NPC is composed of numerous protein subunits referred to as nucleoporins,
Autor:
Michael E. Colvin, Ajay Gopinathan, Timothy G. Connolly, Robert L. Wang, David Ando, Shawn Newsam
Publikováno v:
Biophysical Journal. 106:608a
Analysis tools optimized to study molecular dynamics (MD) simulations of intrinsically disordered proteins (IDPs) are currently rare. We are developing a set of tools using the libraries and interface of the widely used MD simulation software Gromacs