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Thermodynamics of folding, stabilization, and binding in an engineered protein-protein complex

التفاصيل البيبلوغرافية
العنوان: Thermodynamics of folding, stabilization, and binding in an engineered protein-protein complex
المؤلفون: Dincbas-Renqvist, Vildan, Lendel, Christofer, Dogan, Jakob, Wahlberg, Elisabet, Härd, Torleif
المصدر: Journal of the American Chemical Society. 126(36):11220-11230
مصطلحات موضوعية: combinatorial libraries, staphylococcus-aureus, molten globules, affibody, domain, entropy, dna, microcalorimetry, recognition, parameters, TECHNOLOGY, Bioengineering, Structural biochemistry, TEKNIKVETENSKAP, Bioteknik, Strukturbiokemi
الوصف: We analyzed the thermodynamics of a complex protein-protein binding interaction using the (engineered) Z(SPA-1) affibody and it's Z domain binding partner as a model. Free Z(SPA-1) exists in an equilibrium between a molten-globule-like (MG) state and a completely unfolded state, wheras a well-ordered structure is observed in the Z:Z(SPA-1) complex. The thermodynamics of the MG state unfolding equilibrium can be separated from the thermodynamics of binding and stabilization by combined analysis of isothermal titration calorimetry data and a separate van't Hoff analysis of thermal unfolding. We find that (i) the unfolding equilibrium of free Z(SPA-1) has only a small influence on effective binding affinity, that (ii) the Z:Z(SPA-1) interface is inconspicuous and structure-based energetics calculations suggest that it should be capable of supporting strong binding, but that (iii) the conformational stabilization of the MG state to a well-ordered structure in the Z:Z(SPA-1) complex is associated with a large change in conformational entropy that opposes binding.
وصف الملف: print
URL الوصول: https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-6406
http://pubs.acs.org/cgi-bin/abstract.cgi/jacsat/2004/126/i36/abs/ja047727y.html
قاعدة البيانات: SwePub
الوصف
تدمد:00027863
15205126
DOI:10.1021/ja047727y