Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Johan A. Grahnen"'
Publikováno v:
Genes
Genes, Vol 2, Iss 4, Pp 748-762 (2011)
Genes, Vol 2, Iss 4, Pp 748-762 (2011)
Protein sequence, structure, and function are inherently linked through evolution and population genetics. Our knowledge of protein structure comes from solved structures in the Protein Data Bank (PDB), our knowledge of sequence through sequences fou
Autor:
Damir Herman, Vernon T. Phan, Pek Yee Lum, Sidney P. Elmer, Traci Mizuno, Andrew Asher Protter, Brent Louie, Johan A. Grahnen, Kevin H. Kim
Publikováno v:
Journal of Clinical Oncology. 36:e14575-e14575
e14575Background: Reactive oxygen species (ROS) homeostasis is crucial for cell survival. Drugs that possess anti-tumor effects by suppressing ROS metabolism in cancer cells have potential as a new...
Autor:
Joseph W. Thornton, Eugene I. Shakhnovich, Arne Elofsson, A. P. Jason de Koning, Simon C. Lovell, Andrew J. Roger, David D. Pollock, Kimmen Sjölander, Shamil R. Sunyaev, Jesse D. Bloom, Ivet Bahar, Gavin J. P. Naylor, Daniel M. Weinreich, Tina Perica, Richard A. Goldstein, Simon Whelan, Nicholas Lartillot, Nimrod D. Rubinstein, Johan A. Grahnen, Lynne Regan, David A. Liberles, Lucy J. Colwell, Mark T. Holder, Erich Bornberg-Bauer, Ashley I. Teufel, Sarah A. Teichmann, Jeffrey L. Thorne, Clemens Lakner, Tal Pupko, Dietlind L. Gerloff, Ugo Bastolla, Julián Echave, Nikolay V. Dokholyan
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The interface of protein structural biology, protein biophysics, molecular evolution, and molecular population genetics forms the foundations for a mechanistic understanding of many aspects of protein biochemistry. Current efforts in interdisciplinar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b2d846d58eccbbb6e6aa51846bca04d
http://hdl.handle.net/10261/99827
http://hdl.handle.net/10261/99827
Publikováno v:
Computational Modeling of Biological Systems ISBN: 9781461421450
Biological systems span multiple layers of organization and modeling across layers of organization enables inference that is not possible by analyzing just one layer. An example of this is seen in an organism’s fitness, which can be directly impact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::739588aef808386fadba5b6ae9c1afc4
https://doi.org/10.1007/978-1-4614-2146-7_15
https://doi.org/10.1007/978-1-4614-2146-7_15
Publikováno v:
BMC Evolutionary Biology, Vol 11, Iss 1, p 361 (2011)
BMC Evolutionary Biology
BMC Evolutionary Biology
Background Protein sequence evolution is constrained by the biophysics of folding and function, causing interdependence between interacting sites in the sequence. However, current site-independent models of sequence evolutions do not take this into a
A number of biophysical and population-genetic processes influence amino acid substitution rates. It is commonly recognized that proteins must fold into a native structure with preference over an unfolded state, and must bind to functional interactin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f923c11c49a0379e651ee7f9ebe7dd79
https://europepmc.org/articles/PMC3107659/
https://europepmc.org/articles/PMC3107659/
Autor:
Johan A. Grahnen, Jan Kubelka
Publikováno v:
Biophysical Journal. 100(3)
Infrared (IR) amide I’ spectra are widely used for investigations of the structural properties of proteins in aqueous solution. For analysis of the experimental data it is necessary to separate the spectral features due to the backbone conformation
Publikováno v:
Journal of molecular evolution. 73(1-2)
For high-throughput structural genomic and evolutionary bioinformatics approaches, there is a clear need for fast methods to evaluate substitutions structurally. Coarse-grained methods are both powerful and fast, and a coarse-grained approach to posi
Publikováno v:
The journal of physical chemistry. B. 114(40)
Infrared (IR) amide I' spectra are widely used for investigations of the structural properties of proteins in aqueous solution. For analysis of the experimental data, it is necessary to separate the spectral features due to the backbone conformation
Autor:
David A. Liberles, Johan A. Grahnen
Publikováno v:
Trends in Evolutionary Biology. 4:9
CASS (coarse-grained artificial sequence simulator) is a software package for simulating protein sequences with an explicit genotype-to-phenotype mapping that takes protein structure and function into account. It is capable of reproducing many struct