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of 3
pro vyhledávání: '"Mert, Karakas"'
Autor:
Axel W, Fischer, Nathan S, Alexander, Nils, Woetzel, Mert, Karakas, Brian E, Weiner, Jens, Meiler
Publikováno v:
Proteins. 83(11)
For many membrane proteins, the determination of their topology remains a challenge for methods like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. Electron paramagnetic resonance (EPR) spectroscopy has evolved as an alterna
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1112e88604413c7617b5792ec40893cf
https://pubmed.ncbi.nlm.nih.gov/25820805
https://pubmed.ncbi.nlm.nih.gov/25820805
Autor:
Brian E, Weiner, Nathan, Alexander, Louesa R, Akin, Nils, Woetzel, Mert, Karakas, Jens, Meiler
Publikováno v:
Proteins. 82(4)
When experimental protein NMR data are too sparse to apply traditional structure determination techniques, de novo protein structure prediction methods can be leveraged. Here, we describe the incorporation of NMR restraints into the protein structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d4c6eb1da2a8a0038de419144ffcbd50
https://pubmed.ncbi.nlm.nih.gov/24123100
https://pubmed.ncbi.nlm.nih.gov/24123100
Publikováno v:
Proteins. 81(7)
Prediction of transmembrane spans and secondary structure from the protein sequence is generally the first step in the structural characterization of (membrane) proteins. Preference of a stretch of amino acids in a protein to form secondary structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::85ea2c4876b0b5d1d36aee8151f33ed8
https://pubmed.ncbi.nlm.nih.gov/23349002
https://pubmed.ncbi.nlm.nih.gov/23349002