Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape
暂无分享,去创建一个
[1] D. W. Bolen,et al. Anatomy of energetic changes accompanying urea-induced protein denaturation , 2007, Proceedings of the National Academy of Sciences.
[2] Yawen Bai,et al. The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate. , 2007, Journal of molecular biology.
[3] Doug Barrick,et al. An experimentally determined protein folding energy landscape. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[4] M. Proctor,et al. Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots. , 1999, Biochemistry.
[5] C. Pace. Determination and analysis of urea and guanidine hydrochloride denaturation curves. , 1986, Methods in enzymology.
[6] D. Thirumalai,et al. Kinetics of protein folding: Nucleation mechanism, time scales, and pathways , 1995 .
[7] A. Fersht,et al. Mapping the transition state and pathway of protein folding by protein engineering , 1989, Nature.
[8] Andreas Plückthun,et al. Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins. , 2008, Journal of molecular biology.
[9] D. Gillespie. Exact Stochastic Simulation of Coupled Chemical Reactions , 1977 .
[10] Sophie E Jackson,et al. Local and long-range stability in tandemly arrayed tetratricopeptide repeats. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[11] Tommi Kajander,et al. A new folding paradigm for repeat proteins. , 2005, Journal of the American Chemical Society.
[12] Doug Barrick,et al. Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape. , 2008, Journal of the American Chemical Society.
[13] Doug Barrick,et al. Repeat-protein folding: new insights into origins of cooperativity, stability, and topology. , 2008, Archives of biochemistry and biophysics.
[14] B. Matthews,et al. Structure and thermal stability of phage T4 lysozyme. , 1987, Methods in enzymology.
[15] J. Onuchic,et al. Funnels, pathways, and the energy landscape of protein folding: A synthesis , 1994, Proteins.
[16] Hongyi Zhou,et al. Critical nucleation size in the folding of small apparently two‐state proteins , 2004, Protein Science.
[17] Doug Barrick,et al. An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions , 2005, Protein science : a publication of the Protein Society.
[18] P. Wolynes,et al. The experimental survey of protein-folding energy landscapes , 2005, Quarterly Reviews of Biophysics.
[19] T. Huppert,et al. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices. , 2003, Biochemistry.
[20] D. Baker,et al. Contact order, transition state placement and the refolding rates of single domain proteins. , 1998, Journal of molecular biology.
[21] Sheena E Radford,et al. Intermediates: ubiquitous species on folding energy landscapes? , 2007, Current opinion in structural biology.
[22] K. Dill,et al. From Levinthal to pathways to funnels , 1997, Nature Structural Biology.
[23] D. Shortle,et al. Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions. , 1989, Biochemistry.
[24] Z. Peng,et al. Consensus-derived structural determinants of the ankyrin repeat motif , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[25] S Walter Englander,et al. Protein folding and misfolding: mechanism and principles , 2007, Quarterly Reviews of Biophysics.
[26] Kristina M. Cook,et al. Asparaginyl Hydroxylation of the Notch Ankyrin Repeat Domain by Factor Inhibiting Hypoxia-inducible Factor* , 2007, Journal of Biological Chemistry.
[27] S. Jackson,et al. How do small single-domain proteins fold? , 1998, Folding & design.
[28] D. Barrick,et al. Experimental characterization of the folding kinetics of the notch ankyrin domain. , 2005, Journal of molecular biology.
[29] C. Pace,et al. Urea and Guanidine Hydrochloride Denaturation of Ribonuclease , Lysozyme , & Zhymotrypsin , and @ Lactoglobulin * , 2003 .
[30] Doug Barrick,et al. The notch ankyrin domain folds via a discrete, centralized pathway. , 2006, Structure.
[31] Doug Barrick,et al. Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeats. , 2007, Journal of molecular biology.
[32] T. Oas,et al. Reinterpretation of GCN4-p1 folding kinetics: partial helix formation precedes dimerization in coiled coil folding. , 1999, Journal of molecular biology.
[33] Martin Karplus,et al. Application of the diffusion-collision model to the folding of three-helix bundle proteins. , 2002, Journal of molecular biology.
[34] M Karplus,et al. Protein folding dynamics: The diffusion‐collision model and experimental data , 1994, Protein science : a publication of the Protein Society.
[35] Doug Barrick,et al. Predicting coupling limits from an experimentally determined energy landscape , 2007, Proceedings of the National Academy of Sciences.
[36] T. Oas,et al. Protein folding dynamics: quantitative comparison between theory and experiment. , 1998, Biochemistry.
[37] T. Kiefhaber,et al. Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding. , 2002, Biophysical chemistry.
[38] D. Gillespie. A General Method for Numerically Simulating the Stochastic Time Evolution of Coupled Chemical Reactions , 1976 .
[39] M. Tsai,et al. Dissection of protein-protein interaction and CDK4 inhibition in the oncogenic versus tumor suppressing functions of gankyrin and P16. , 2007, Journal of molecular biology.
[40] D. W. Bolen,et al. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. , 1988, Biochemistry.
[41] Peter G Wolynes,et al. The energy landscape of modular repeat proteins: topology determines folding mechanism in the ankyrin family. , 2005, Journal of molecular biology.
[42] H. Dyson,et al. Transfer of flexibility between ankyrin repeats in IkappaB* upon formation of the NF-kappaB complex. , 2008, Journal of molecular biology.
[43] D Baker,et al. Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics. , 2000, Biochemistry.
[44] C. Pace,et al. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. , 1974, The Journal of biological chemistry.
[45] D. Barrick,et al. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties. , 2001, Biochemistry.
[46] Doug Barrick,et al. Effect of multiple prolyl isomerization reactions on the stability and folding kinetics of the notch ankyrin domain: experiment and theory. , 2005, Journal of molecular biology.
[47] Doug Barrick,et al. Structure and stability of the ankyrin domain of the Drosophila Notch receptor , 2003, Protein science : a publication of the Protein Society.
[48] Doug Barrick,et al. Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat. , 2002, Journal of molecular biology.
[49] J. Takei,et al. Absence of stable intermediates on the folding pathway of barnase. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[50] Terrence G. Oas,et al. Preorganized secondary structure as an important determinant of fast protein folding , 2001, Nature Structural Biology.