دورية أكاديمية

Metastability of native proteins and the phenomenon of amyloid formation

التفاصيل البيبلوغرافية
العنوان: Metastability of native proteins and the phenomenon of amyloid formation
المؤلفون: Baldwin A. J., Knowles T. P. J., Tartaglia G. G., Fitzpatrick A. W., Devlin G. L., Shammas S. L., Waudby C. A., Mossuto M. F., Meehan S., Gras S. L., Christodoulou J., Anthony-Cahill S. J., Barker P. D., Vendruscolo M., Dobson C. M.
المساهمون: Baldwin, A. J., Knowles, T. P. J., Tartaglia, G. G., Fitzpatrick, A. W., Devlin, G. L., Shammas, S. L., Waudby, C. A., Mossuto, M. F., Meehan, S., Gras, S. L., Christodoulou, J., Anthony-Cahill, S. J., Barker, P. D., Vendruscolo, M., Dobson, C. M.
بيانات النشر: AMER CHEMICAL SOC
1155 16TH ST, NW, WASHINGTON, DC 20036 USA
سنة النشر: 2011
المجموعة: Sapienza Università di Roma: CINECA IRIS
مصطلحات موضوعية: Amyloid, Animal, Cattle, Entropy, Human, Protein Conformation, Protein Stability
الوصف: An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable. © 2011 American Chemical Society.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/21650202; info:eu-repo/semantics/altIdentifier/wos/WOS:000295193700004; volume:133; issue:36; firstpage:14160; lastpage:14163; numberofpages:4; journal:JOURNAL OF THE AMERICAN CHEMICAL SOCIETY; http://hdl.handle.net/11573/1451766Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-80052555139
DOI: 10.1021/ja2017703
الإتاحة: https://doi.org/10.1021/ja2017703Test
http://hdl.handle.net/11573/1451766Test
حقوق: info:eu-repo/semantics/openAccess
رقم الانضمام: edsbas.93377D15
قاعدة البيانات: BASE