Protein apomyoglobin

Privalov et al (1989) studied the unfolded forms of several globular proteins [ribonuclease A, hen egg white lysozyme, apomyoglobin (apoMb), cytochrome c, and staphylococcal nuclease]. Unfolding was induced by 6 M Gdm-HCl at 10°C, heating to 80°C, or by low pH at 10°C with cross-links cleaved (reduction and carboxamidomethylation or removal of heme). The unfolded forms showed CD spectra (Fig. 27)... 

A. Probing the Protein Folding Landscape Equilibrium NMR Studies of Apomyoglobin... 

Eliezer D., Yao J., Dyson H. J. and Wright P. E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. (1998) 5(2) 148-155. 

Ballew R. M., Sabelko J. and Gruebele M. Direct observation of fast protein folding the initial collapse of apomyoglobin. Proc. Natl. Acad. Sri., USA (1996) 93 5759-5764. 

Gilmanshin R., Williams S., Callender R. H., Woodruff W. H. and Dyer R. B. Fast events in protein folding relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci., USA (1997) 94(8) 3709-3713. 

Bismuto et alF compared the phosphorescence from both tuna and sperm whale apomyoglobin. The emission occurs from a tryptophan in the A helix. The temperature dependence of lifetime and the position of the 0-0 vibrational band differ as a function of temperature for the two proteins. The authors interpreted their results to indicate that the microenvironment of the tryptophan in sperm whale apomyoglobin possesses a higher degree of internal flexibility than that in the tuna protein. 

Transfer capillary, glass chip EOF ESI-ITMS Tryptic digest of horse apomyoglobin (7.4 nM), yeast proteins Trypsin Non-chip gradient frontal CEC separation C18 column 803... 

Direct MD simulations of the observed Stokes shifts and corresponding solvation time scales for several proteins were reported recently [188, 199, 202, 203]. Overall, significant discrepancies exist between simulation results and experimental observations, but some general features are promising. Here, we summarize one of our recent MD studies of W7 in apomyoglobin with linear response and direct nonequilibrium calculations and highlight the critical findings, as well as point out extensive improvement required in theoretical model [199]. 

Application of Equation (13.8) is correct when the ligand (here ethidium bromide) is very small compared to the macromolecule (DNA) and when the ligand binds almost completely when it is added to the macromolecule. This was observed also for the interaction between hemin and apomyoglobin or apocytochrome, and between TNS and almost all proteins. 

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