Christopher M Bruns
Overview
Explore the profile of Christopher M Bruns including associated specialties, affiliations and a list of published articles.
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6
Citations
634
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Recent Articles
1.
Eastman P, Friedrichs M, Chodera J, Radmer R, Bruns C, Ku J, et al.
J Chem Theory Comput
. 2013 Jan;
9(1):461-469.
PMID: 23316124
OpenMM is a software toolkit for performing molecular simulations on a range of high performance computing architectures. It is based on a layered architecture: the lower layers function as a...
2.
Flores S, Sherman M, Bruns C, Eastman P, Altman R
IEEE/ACM Trans Comput Biol Bioinform
. 2011 Jul;
8(5):1247-57.
PMID: 21778523
Modeling the structure and dynamics of large macromolecules remains a critical challenge. Molecular dynamics (MD) simulations are expensive because they model every atom independently, and are difficult to combine with...
3.
Friedrichs M, Eastman P, Vaidyanathan V, Houston M, LeGrand S, Beberg A, et al.
J Comput Chem
. 2009 Feb;
30(6):864-72.
PMID: 19191337
We describe a complete implementation of all-atom protein molecular dynamics running entirely on a graphics processing unit (GPU), including all standard force field terms, integration, constraints, and implicit solvent. We...
4.
Garcin E, Bruns C, Lloyd S, Hosfield D, Tiso M, Gachhui R, et al.
J Biol Chem
. 2004 Jun;
279(36):37918-27.
PMID: 15208315
Three nitric-oxide synthase (NOS) isozymes play crucial, but distinct, roles in neurotransmission, vascular homeostasis, and host defense, by catalyzing Ca(2+)/calmodulin-triggered NO synthesis. Here, we address current questions regarding NOS activity...
5.
Cardoso R, Daniels D, Bruns C, Tainer J
Proteins
. 2003 Feb;
51(1):137-46.
PMID: 12596270
The 26-kDa glutathione S-transferase from Schistosoma japonicum (Sj26GST), a helminth worm that causes schistosomiasis, catalyzes the conjugation of glutathione with toxic secondary products of membrane lipid peroxidation. Crystal structures of...
6.
Abdalla A, Bruns C, Tainer J, Mannervik B, Stenberg G
Protein Eng
. 2002 Dec;
15(10):827-34.
PMID: 12468717
By the introduction of 10 site-specific mutations in the dimer interface of human glutathione transferase P1-1 (GSTP1-1), a stable monomeric protein variant, GSTP1, was obtained. The monomer had lost the...