Myoglobin studies

Nilsson K et al (2004) The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations quantum refinement. Biophys J 87(5) 3437-3447... 

Fig. 8. A view into the interior of a ruthenium modified myoglobin where the amino acids in the vicinity of Trp-14 are shown. The dots correspond to the statistieal density Pn i,(r) of (discretized) tunneling path vertices (rj in Eq. 26) from 500,000 tunneling paths [19], The (r) is clustered in a cylindrical zone centered on the average path, shown as the light line appearing in the center and emerging toward the viewer. The computation modeled paths of electron transfer in Ru(His-12) myoglobin studied experimentally by Gray and coworkers [88]...

Doster, W., and Gebhardt, R. (2003) High pressure-unfolding of myoglobin studied by dynamic neutron scattering, Chem. Phys. 292, 383-387... 

Morrow, J. S., Keim, P., and Gurd, F. R. N. (1974). J. Biol. Chem. 249, 7484. CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon-13 and Proton Nuclear Magnetic Resonance. 

Simmons, D.A., Dunn, S.D., Konermann, L. (2003) Conformational dyneunics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange. Biochemistry, 42 (19), 5896-5905. 

Konermann, L Rosell, F.I., Mauk, A.G., Douglas, D.J. (1997) Acid-induced Denat-uration of Myoglobin Studied by Time-resolved Electrospray Ionization Mass Spectrometry. Biochemistry 36 6448-6454. 

Schenk, E.R., Almeida, R., Miksovska, J., Ridgeway, M.E., Park, M.A., Fernandez-Lima, F. (2015) Kinetic Intermediates of Holo- and Apo-myoglobin Studied Using HDX-TIMS-MS and Molecular Dynamic Simulations. J. Am. Soc. Mass Spectrom. 

Asher S A and Chi Z H 1998 UV resonance Raman studies of protein folding in myoglobin and other proteins Biophys. 

Rella C W, Rector K D, Kwok A, Hill J R, Schwettman H A, DIott D D and Fayer M D 1996 Vibrational echo studies of myoglobin-CO J. Phys. Chem. 100 15 620-29... 

The problems that occur when one tries to estimate affinity in terms of component terms do not arise when perturbation methods are used with simulations in order to compute potentials of mean force or free energies for molecular transformations simulations use a simple physical force field and thereby implicitly include all component terms discussed earlier. We have used the molecular transformation approach to compute binding affinities from these first principles [14]. The basic approach had been introduced in early work, in which we studied the affinity of xenon for myoglobin [11]. The procedure was to gradually decrease the interactions between xenon atom and protein, and compute the free energy change by standard perturbation methods, cf. (10). An (issential component is to impose a restraint on the... 

PSS-SG composite film was tested for sorption of heme proteins hemoglobin (Hb) and myoglobin (Mb). The peroxidaze activity of adsorbed proteins were studied and evaluated by optical and voltammetric methods. Mb-PSS-SG film on PG electrode was shown to be perspective for detection of dissolved oxygen and hydrogen peroxide by voltammetry with linear calibration in the range 2-30 p.M, and detection limit -1.5 p.M. Obtained composite films can be modified by different types of biological active compounds which is important for the development of sensitive elements of biosensors. 

As described in Chapter 2, the first complete protein structure to be determined was the globular protein myoglobin. However, the a helix that was recognized in this structure, and which has emerged as a persistent structural motif in the many hundreds of globular proteins determined subsequently, was first observed in x-ray diffraction studies of fibrous proteins. 

As noted, hemoglobin is an tetramer. Each of the four subunits has a conformation virtually identical to that of myoglobin. Two different types of subunits, a and /3, are necessary to achieve cooperative Oa-binding by Hb. The /3-chain at 146 amino acid residues is shorter than the myoglobin chain (153 residues), mainly because its final helical segment (the H helix) is shorter. The a-chain (141 residues) also has a shortened H helix and lacks the D helix as well (Figure 15.28). Max Perutz, who has devoted his life to elucidating the atomic structure of Hb, noted very early in his studies that the molecule was... 

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