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pro vyhledávání: '"Emilio Jimenez-Roldan"'
Autor:
J. Emilio Jimenez-Roldan, Saraswathi Vishweshwara, Robert B. Freedman, Moitrayee Bhattacharyya, Rudolf A. Römer, Stephen A. Wells
Publikováno v:
Proteins
We have studied the mobility of the multidomain folding catalyst, protein disulfide isomerase (PDI), by a coarse‐graining approach based on flexibility. We analyze our simulations of yeast PDI (yPDI) using measures of backbone movement, relative po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b252377d8a498b8b525801066c0ff7b
http://wrap.warwick.ac.uk/81247/7/WRAP_R-mer_et_al-2016-Proteins-_Structure,_Function,_and_Bioinformatics.pdf
http://wrap.warwick.ac.uk/81247/7/WRAP_R-mer_et_al-2016-Proteins-_Structure,_Function,_and_Bioinformatics.pdf
Autor:
Peter J. Sadler, Stephen A. Wells, J. Emilio Jimenez-Roldan, Huilin Li, Peter B. O’Connor, Yao Zhao, Rudolf A. Römer
Publikováno v:
Protein Science. 21:1269-1279
Chemical crosslinking in combination with Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) has significant potential for studying protein structures and protein–protein interactions. Previously, cisplatin has been shown to be
Autor:
David T. Clarke, Narinder Sanghera, John Blood, Robert B. Freedman, Rudolf A. Roemer, Emilio Jimenez-Roldan, Jack W. Heal
Publikováno v:
Biophysical Journal. 106(2)
PDI is an abundant folding catalyst and chaperone, required for formation of native disulfide bonds in secretory proteins. PDI interacts with many redox partners in the oxidative protein folding pathway and acts on an immense range of unfolded and pa
Rigidity analysis using the "pebble game" has been applied to protein crystal structures to obtain information on protein folding, assembly and t he structure-function relationship. However, previous work using this technique has not made clear how t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7da30ed18f7fcc34671915740cca539
Autor:
Römer, Rudolf A., Wells, Stephen A., Emilio Jimenez‐Roldan, J., Bhattacharyya, Moitrayee, Vishweshwara, Saraswathi, Freedman, Robert B.
Publikováno v:
Proteins; Dec2016, Vol. 84 Issue 12, p1776-1785, 10p
Publikováno v:
Journal of Physics: Conference Series. 286:012002
Our simulations of protein motion are based on a rigidity-based coarse graining criteria which is able to identify flexible and constraint regions and on Normal Modes of Motion (NMM) which map out the directions of motion for a given network. The NMM