کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2189418 1096210 2006 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Electrostatic Interactions in the Denatured State and in the Transition State for Protein Folding: Effects of Denatured State Interactions on the Analysis of Transition State Structure
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
Electrostatic Interactions in the Denatured State and in the Transition State for Protein Folding: Effects of Denatured State Interactions on the Analysis of Transition State Structure
چکیده انگلیسی

The development of electrostatic interactions during the folding of the N-terminal domain of the ribosomal protein L9 (NTL9) is investigated by pH-dependent rate equilibrium free energy relationships. We show that Asp8, among six acidic residues, is involved in non-native, electrostatic interactions with K12 in the transition state for folding as well as in the denatured state. The perturbed native state pKa of D8 (pKa = 3.0) appears to be maintained through non-native interactions in both the transition state and the denatured state. Mutational effects on the stability of the transition state for protein (un)folding are often analyzed in respect to change in ground states. Thus, the interpretation of transition state analysis critically depends on an understanding of mutational effects on both the native and denatured state. Increasing evidence for structurally biased denatured states under physiological conditions raises concerns about possible denatured state effects on folding studies. We show that the structural interpretation of transition state analysis can be altered dramatically by denatured state effects.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 359, Issue 5, 23 June 2006, Pages 1437–1446
نویسندگان
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