Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Thomas, Wüst"'
Publikováno v:
American Journal of Physics. 87:310-316
We describe a minimalistic model of a protein undergoing folding into its native (ground) state. This HP protein model is composed of a lattice polymer with two types of monomers: hydrophobic (H) and polar (P). The specific sequence of the two types
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a5b0ce1cfd791d54b2178e2e2cb663c
https://doi.org/10.1119/1.5093292
https://doi.org/10.1119/1.5093292
Autor:
Diana, Coman Schmid, Katrin, Crameri, Sabine, Oesterle, Bernd, Rinn, Thierry, Sengstag, Heinz, Stockinger, Thomas, Wüst
Publikováno v:
Studies in health technology and informatics. 270
The BioMedIT project is funded by the Swiss government as an integral part of the Swiss Personalized Health Network (SPHN), aiming to provide researchers with access to a secure, powerful and versatile IT infrastructure for doing data-driven research
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a2596e6b23b6c789f1461f17a0d322ef
https://pubmed.ncbi.nlm.nih.gov/32570566
https://pubmed.ncbi.nlm.nih.gov/32570566
Publikováno v:
Molecular Simulation. 44:1025-1030
With the highly simplified hydrophobic-polar model representation of a protein, we can study essential qualitative physics without an unnecessarily large computational overhead. Using Wang-Landau s...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9564f823af9a82691029f3577c155cea
https://doi.org/10.1080/08927022.2018.1471691
https://doi.org/10.1080/08927022.2018.1471691
Publikováno v:
Journal of Physics: Conference Series, 1290 (1)
To compare folding behavior among lattice proteins which have similar corresponding structures in nature, Crambin homologues are tested in the semi-flexible H0P lattice model using replica-exchange Wang-Landau sampling. Our simulation shows that, at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d88e9302dc543f846619551b2b5b0e8b
We describe a class of "bare bones" models of homopolymers which undergo coil-globule collapse and proteins which fold into their native states in free space or into denatured states when captured by an attractive substrate as the temperature is lowe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6c5d0c0631e94ed833566d93c82e7e3
http://doc.rero.ch/record/316444/files/10955_2011_Article_266.pdf
http://doc.rero.ch/record/316444/files/10955_2011_Article_266.pdf
Publikováno v:
Batagiannis, Athanasios; Wüst, Thomas; Hulliger, Jürg (2009). Universality behaviour for polarity formation in channel-type inclusion compounds. Journal of mathematical chemistry, 45(4), pp. 882-883. Springer Netherlands 10.1007/s10910-008-9469-1
Batagiannis, Athanasios; Wüst, Thomas; Hulliger, Jürg (2009). Universality behaviour for polarity formation in channel-type inclusion compounds. Journal of mathematical chemistry, 45(4), pp. 869-881. Bussum: Springer Netherlands 10.1007/S10910-008-9433-0
Batagiannis, Athanasios; Wüst, Thomas; Hulliger, Jürg (2009). Universality behaviour for polarity formation in channel-type inclusion compounds. Journal of mathematical chemistry, 45(4), pp. 869-881. Bussum: Springer Netherlands 10.1007/S10910-008-9433-0
A statistical investigation based on a Markov chain theory of polarity formation applied to channel-type inclusion compounds loaded with both dipolar A–π–D and non-polar N–π–N (N: A or D) guests is presented. The key parameters effecting po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aecac0869342c1d2ebf5820237e9bedb
http://doc.rero.ch/record/319578/files/10910_2008_Article_9433.pdf
http://doc.rero.ch/record/319578/files/10910_2008_Article_9433.pdf
Autor:
Christian Beisel, Gerhard Christofori, Ariane L. Hofmann, Thomas Wüst, Thomas Thurnherr, Daniel J. Stekhoven, Nora C. Toussaint, Holger Moch, Reinhard Dummer, Mitchell P. Levesque, Niko Beerenwinkel, Charlotte K.Y. Ng, Salvatore Piscuoglio, F. Singer, Jochen Singer, Bernd Rinn, Peter J. Wild, Andreas Papassotiropoulos, Markus G. Manz, Wilhelm Krek, Michael N. Hall, Hans-Joachim Ruscheweyh
Publikováno v:
Bioinformatics, 34 (1)
Bioinformatics
Bioinformatics
Motivation Next-generation sequencing is now an established method in genomics, and massive amounts of sequencing data are being generated on a regular basis. Analysis of the sequencing data is typically performed by lab-specific in-house solutions,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::204a8126a1f41b186b3a8f73c8512e85
Publikováno v:
Journal of Physics: Conference Series, 1012 (1)
Many studies inspired by the HP lattice protein model have helped to confirm the importance of the hydrophobic "driving force" during folding. Unfortunately, the high level of coarse-graining inherent to this model leads to significant limitations; r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf926d7b941ca9eee5a27ac8186d40a1
Publikováno v:
Hulliger, Jürg; Wüst, Thomas; Rech, Mathias (2013). Symmetry and the polar state of condensed molecular matter. Zeitschrift für Kristallographie, 228(12), pp. 607-610. OLDENBOURG WISSENSCHAFTSVERLAG 10.1524/zkri.2013.1654
Polar molecular crystals seem to contradict a quantum mechanical statement, according to which no stationary state of a system features a permanent electrical polarization. By stationary we understand here an ensemble for which thermal averaging appl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43c45e2cc9b2849035fe45d8a83b31ee
http://doc.rero.ch/record/292983/files/zkri-2014-5002.pdf
http://doc.rero.ch/record/292983/files/zkri-2014-5002.pdf
Publikováno v:
Molecular Simulation. 40:640-655
Generic features associated with the adsorption of proteins on solid surfaces are reviewed within the framework of the hydrophobic-polar (HP) lattice protein model. The thermodynamic behaviour and ...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::563e7fcf5e42c4bb219abfd3e29fa2e8
https://doi.org/10.1080/08927022.2013.847273
https://doi.org/10.1080/08927022.2013.847273