Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?
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[1] M. Brunori,et al. Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain* , 2016, The Journal of Biological Chemistry.
[2] Guruswamy Krishnamoorthy,et al. Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state. , 2013, Biophysical journal.
[3] Alexander Tischer,et al. Urea‐temperature phase diagrams capture the thermodynamics of denatured state expansion that accompany protein unfolding , 2013, Protein science : a publication of the Protein Society.
[4] M. Jagannadham,et al. Evidence for a Molten Globule State in Cicer α-Galactosidase Induced by pH, Temperature, and Guanidine Hydrochloride , 2013, Applied Biochemistry and Biotechnology.
[5] M. Waegele,et al. Spectroscopic studies of protein folding: Linear and nonlinear methods , 2012, Protein science : a publication of the Protein Society.
[6] A. Finkelstein,et al. How strong are side chain interactions in the folding intermediate? , 2009, Protein science : a publication of the Protein Society.
[7] K. Soda,et al. The compact and expanded denatured conformations of apomyoglobin in the methanol‐water solvent , 2008, Protein science : a publication of the Protein Society.
[8] Shuji Akiyama,et al. Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR , 2008, Proceedings of the National Academy of Sciences.
[9] Satoshi Takahashi,et al. Solvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy. , 2007, Journal of molecular biology.
[10] A. Finkelstein,et al. Three‐state protein folding: Experimental determination of free‐energy profile , 2005, Protein science : a publication of the Protein Society.
[11] D. Barrick,et al. Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[12] Gerard J A Kroon,et al. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. , 2004, Journal of molecular biology.
[13] H. Dyson,et al. Molecular hinges in protein folding: the urea-denatured state of apomyoglobin. , 2002, Biochemistry.
[14] H. Dyson,et al. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. , 2001, Biochemistry.
[15] R. L. Baldwin,et al. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. , 1998, Biochemistry.
[16] H. Jane Dyson,et al. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding , 1998, Nature Structural Biology.
[17] P. Wright,et al. Is apomyoglobin a molten globule? Structural characterization by NMR. , 1996, Journal of molecular biology.
[18] Y. Kao,et al. The native state of apomyoglobin described by proton NMR spectroscopy: The A‐B‐G‐H interface of wild‐type sperm whale apomyoglobin , 1996, Proteins.
[19] Robert L. Baldwin,et al. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin , 1996, Nature Structural Biology.
[20] O. Ptitsyn,et al. Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. , 1996, Biochemistry.
[21] Michael S. Kay,et al. Packing interactions in the apomyglobin folding intermediate , 1996, Nature Structural Biology.
[22] P. Privalov,et al. Thermodynamic puzzle of apomyoglobin unfolding. , 1994, Journal of molecular biology.
[23] R. L. Baldwin,et al. The molten globule intermediate of apomyoglobin and the process of protein folding , 1993, Protein Science.
[24] A. Fink,et al. Phase diagram for acidic conformational states of apomyoglobin. , 1990, Journal of molecular biology.
[25] P. Privalov,et al. Thermodynamic study of the apomyoglobin structure. , 1988, Journal of molecular biology.
[26] O. Ptitsyn,et al. Molten globule and protein folding. , 1995, Advances in protein chemistry.
[27] P. Wright,et al. Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances. , 1995, Journal of biomolecular NMR.
[28] C. Tanford. Protein denaturation. , 1968, Advances in protein chemistry.
[29] E. Blout,et al. REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN. , 1965, The Journal of biological chemistry.