Proteins myoglobin

Most potential energy surfaces are extremely complex. Fiber and Karplus analyzed a 300 psec molecular dynamics trajectory of the protein myoglobin. They estimate that 2000 thermally accessible minima exist near the native protein structure. The total number of conformations is even larger. Dill derived a formula to calculate the upper bound of thermally accessible conformations in a protein. Using this formula, a protein of 150 residues (the approx-... 

Quasi-molecular ions, [M + nH], from a protein (myoglobin) of molecnlar mass 16,951.5 Da. In this case, n ranges from 21 (giving a measured mass of 808.221) to 12 (corresponding to a measured mass of 1413.631). The peaks with measured masses in between these correspond to the other values of n between 12 and 21. By taking snccessive pairs of measnred masses, the relative molecular mass of the myoglobin can be calculated very accurately, as shown in Figure 8.4. 

The sacroplasmic proteins myoglobin and hemoglobin are responsible for much of the color in meat. Species vary tremendously in the amount of sacroplasmic proteins within skeletal muscle with catde, sheep, pigs, and poultry Hsted in declining order of sarcoplasmic protein content. Fat is also an important component of meat products. The amount of fat in a portion of meat varies depending on the species, anatomy, and state of nutrition of the animal. The properties of processed meat products are greatiy dependent on the properties of the fat included. Certain species, such as sheep, have a relatively higher proportion of saturated fat, whereas other species, such as poultry, have a relatively lower proportion of saturated fat. It is well known that the characteristic davors of meat from different species are in part determined by their fat composition. 

Watson, H.C. The stereochemistry of the protein myoglobin. Progr. Stereochem. 4 299-333, 1969. 

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. 

The different pore sizes and exclusion limits of each TSK-GEL SW column will have a substantial effect on the resolution of a biomolecule mixture. G2000SW packing, which has the smallest pores, provides the best resolution for smaller proteins such as myoglobin and cytochrome c (16,900 and 12,400 Da, respectively, Rs = 1.01). Resolution of the proteins myoglobin... 

Jiang and Zhu (2000) and Qiu and Zhu (2001) have reported the fabrication of multilayered devices composed of stacks of compression-molded disks of alternating compositions. One type of disk is either P(SA-EG) or P[SA-co-TMAgly)-Z>-EG] and the other is a pH-sensitive, protein-loaded blend of, for example, poly(methacrylic acid) and polyethoxazoline. The release of model proteins, myoglobin, bovine serum albumin, and FITC-dextran, and compounds such as brilliant blue have been studied and pulsatile release profiles have been demonstrated (Jiang and Zhu, 2000 Qiu and Zhu, 2001). 

Mixture of proteins (Myoglobin, Ovalbumin, Lysozyme and Chymotrypsinogen) Purification Hydrophobic Interaction [52]... 

The interaction of Fe(II) with small molecules has received much attention. The Fe(II)/ oxygen system must be one of the most studied chemical interactions. Since the Fe-porphyrin complex forms the core of the naturally occurring iron respiratory proteins myoglobin and... 

The first three-dimensional structure of a protein determined was the dioxygen transporter myoglobin isolated from sperm whale in the ferric form (86, 87). A 153 amino acid globular protein, myoglobin contains eight helical regions (A to H) with a single heme b bound between helices... 

Red fibers provide for their ATP requirements mainly (but not exclusively) from fatty acids, which are broken down via 3-oxidation, the tricarboxylic acid cycle, and the respiratory chain (right part of the illustration). The red color in these fibers is due to the monomeric heme protein myoglobin, which they use as an O2 reserve. Myoglobin has a much higher af nity for O2 than hemoglobin and therefore only releases its O2 when there is a severe drop in O2 partial pressure (cf p.282). 

Q Oxygen-Binding Proteins—Myoglobin Oxygen Storage... 

The elucidation of the structure of ribonuclcasc follows that of lycozyme by a group at London s Royal Institute headed by Dr. David C. Phillips, and that of the other protein, myoglobin, for which Dr. Max F. Perutz and Dr. John C. Kendrew of Cambridge University received the Nobel Prize in chemistry in 1962. 

The applicability of the theoretical expressions discussed above has been tested with different systems such as the oxidation of protein myoglobin in the presence of sodium ascorbate [96] or the oxidation of ferrocene in the presence of potassium ferrocyanide [95]. The case corresponding to ferrocene-containing monolayers on a gold electrode in the presence of potassium ferrocyanide will be addressed here. 

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