Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Phineus R. L. Markwick"'
Publikováno v:
Biophysical journal, vol 116, iss 1
Amide hydrogen/deuterium exchange mass spectrometry (HDXMS) of proteins has become extremely popular for identifying ligand-binding sites, protein-protein interactions, intrinsic disorder, and allosteric changes upon protein modification. Such phenom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cea9e3186b67fd881233cf10abc4fffa
https://doi.org/10.1016/j.bpj.2018.11.023
https://doi.org/10.1016/j.bpj.2018.11.023
Autor:
Vladimir Vacic, Phineus R L Markwick, Christopher J Oldfield, Xiaoyue Zhao, Chad Haynes, Vladimir N Uversky, Lilia M Iakoucheva
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 10, p e1002709 (2012)
The effects of disease mutations on protein structure and function have been extensively investigated, and many predictors of the functional impact of single amino acid substitutions are publicly available. The majority of these predictors are based
Externí odkaz:
https://doaj.org/article/84b0f8d58a1e4698b30be8c845f500bd
Publikováno v:
PLoS Computational Biology, Vol 4, Iss 9, p e1000168 (2008)
The function of bio-macromolecules is determined by both their 3D structure and conformational dynamics. These molecules are inherently flexible systems displaying a broad range of dynamics on time-scales from picoseconds to seconds. Nuclear Magnetic
Externí odkaz:
https://doaj.org/article/2639fef1a7c74c3c972fe0fe62641887
Publikováno v:
Biochemistry. 57(18)
Thrombin normally cleaves fibrinogen to promote coagulation, however, binding of thrombomodulin to thrombin switches the specificity of thrombin toward protein C, triggering the anticoagulation pathway. The W215A thrombin mutant was reported to have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8db6a87053ed3914d7ccacbfdbcdd2a
https://pubmed.ncbi.nlm.nih.gov/29634247
https://pubmed.ncbi.nlm.nih.gov/29634247
Autor:
Phineus R. L. Markwick, Marco Tonelli, Brian Fuglestad, Elizabeth A. Komives, Kyle N. Stearns, R. Bryn Fenwick, Lindsey D. Handley
Publikováno v:
Scientific Reports
Although serine proteases are found ubiquitously in both eukaryotes and prokaryotes, and they comprise the largest of all of the peptidase families, their dynamic motions remain obscure. The backbone dynamics of the coagulation serine protease, apo-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49f440ed872f7292fdc844a7b10cb17b
http://europepmc.org/articles/PMC5216386
http://europepmc.org/articles/PMC5216386
Autor:
Elizabeth A. Komives, J. Andrew McCammon, Paul M. Gasper, Phineus R. L. Markwick, Brian Fuglestad
Publikováno v:
Fuglestad, B; Gasper, PM; McCammon, JA; Markwick, PRL; & Komives, EA. (2013). Correlated motions and residual frustration in thrombin. Journal of Physical Chemistry B, 117(42), 12857-12863. doi: 10.1021/jp402107u. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/4c5991x1
The journal of physical chemistry. B, vol 117, iss 42
The Journal of Physical Chemistry. B
The journal of physical chemistry. B, vol 117, iss 42
The Journal of Physical Chemistry. B
Thrombin is the central protease in the cascade of blood coagulation proteases. The structure of thrombin consists of a double β-barrel core surrounded by connecting loops and helices. Compared to chymotrypsin, thrombin has more extended loops that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02e7701ae338dd604bc22fb99e57ca52
https://doi.org/10.1021/jp402107u
https://doi.org/10.1021/jp402107u
Autor:
Phineus R. L. Markwick, Juan Manuel Ortiz-Sánchez, J. Andrew McCammon, Denis Bucher, Levi C. T. Pierce
Publikováno v:
Journal of chemical theory and computation, vol 8, iss 8
Journal of Chemical Theory and Computation
Journal of Chemical Theory and Computation
In the present work, we employ excited state accelerated ab initio molecular dynamics (A-AIMD) to efficiently study the excited state energy landscape and photophysical topology of a variety of molecular systems. In particular, we focus on two import
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99a087aafc349adbc442aa387ffe120e
https://doi.org/10.1021/ct200740r
https://doi.org/10.1021/ct200740r
Autor:
Phineus R. L. Markwick, Michael Nilges
Publikováno v:
Chemical Physics. 396:124-134
Experimental studies of protein structure and dynamics with NMR provide the classical example of the power of theoretical approaches for the interpretation of experimental results. In this paper we review recent developments in experimental technique
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b38fa6702d424a7cd9f6ea78297cdb9e
https://doi.org/10.1016/j.chemphys.2011.11.023
https://doi.org/10.1016/j.chemphys.2011.11.023
Publikováno v:
Journal of Chemical Theory and Computation
Accelerated molecular dynamics (aMD) is an enhanced sampling technique that expedites conformational space sampling by reducing the barriers separating various low-energy states of a system. Here, we present the first application of the aMD method on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02b7a3da837012cccafe4920ad6c6d75
https://doi.org/10.1021/ct200430c
https://doi.org/10.1021/ct200430c
Studying Partially Folded and Intrinsically Disordered Proteins Using NMR Residual Dipolar Couplings
Autor:
Pau Bernadó, Loïc Salmon, Malene Ringkjøbing Jensen, Martin Blackledge, Phineus R. L. Markwick, Gabrielle Nodet
Publikováno v:
Protein NMR Spectroscopy: Practical Techniques and Applications
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a8298a0ad6c5c5a1e9cb31dc2489274
https://doi.org/10.1002/9781119972006.ch9
https://doi.org/10.1002/9781119972006.ch9