Proteins calculations

R/Ro)soiv(f/fo)ellip = n + (mib/m2)(P2/Pi)] (f/fo)eiiip-Briefly justify this expansion of the (f/fo oiv factor. Assuming these particles were solvated to the extent of 0.26 g water (g protein)", calculate (f/fo)eiHp-For prolate ellipsoids of revolution (b/a < 1), Perrin has derived the following expression ... 

C03-0023. Twenty different amino acids are the essential building blocks of proteins. Calculate the molar masses of these three. 

Protein calculator for calculation of, for example, charge, molecular weight, ultraviolet absorption, and some other parameters. 

In zinc-deficient rats, the zinc content of the epididymis was only about half the normal value,28,87 and the level of a-D-mannosidase activity was also little over half the value usually observed.26 However, the zinc concentration of the tissue was still in vast excess over that required for stoichiometric combination with the enzyme protein, calculated on any probable estimate of its specific activity and molecular weight (see Section III,5 p. 433). 

Thermodynamics of Proteins Calculating the Entropy of a Helix-Coil Transition in a Small Antibacterial Peptide using Statistical Mechanics (J. Mol. Bio. 1999, 294, 785-794. "Thermodynamics of the a-Helix-Coil Transition of Amphipathic Peptides in a Membrane Environment Implications for the Peptide-Membrane Binding Equilibrium")... 

Figure 11.3 The interaction energies of two hydrogen atoms and two (tetrahedral) carbon atoms in a protein. (Calculated from the data in Table 11.3.)...

The voluminosity or hydration of interfacially bound protein may be calculated from the amount of water bound per gram of fat divided by the amount of protein bound per gram of fat. This corresponds to the volume of water per gram interfacial protein. Calculations show that emulsifiers facilitate interfacial protein hydration. This property is probably connected with their ability to desorb protein from the interface (Figure 14). 

Coll. = collagen CS = chondroitin sulfate KS = keratan sulfate (calculated from glucosamine values) SA = sialic acid OP = other protein, calculated from total nitrogen - (collagen + hexosamine nitrogen). 

In this paper, the results of a systematic study of the refractive indices of the amino acids, and some peptides and proteins, are described. The value for the refractive index of a protein calculated from the refractive increments of its amino acid residues and solution volume agrees with the experimental value and is a characteristic of the protein. The change in the refractive index of a protein as a result of denaturation has also been investigated. 

A protein, MW 35,000, at a concentration of 0.5 mg/mL, is dialyzed against a ligand at an initial concentration of 4 x 10 5M. At equilibrium, the ligand concentration in the protein compartment is 2.3 x 10 5M, and it is 1.7 x 10"5M in the initial compartment, which contains no protein. Calculate the association constant for the interaction. Assume a single protein-ligand binding site. 

Assay Acid Casein Not less than 90.0% protein Rennet Casein Not less than 86.0% protein Caseinate Salts Not less than 84.0% protein, calculated on the dried basis. 

Assay Not less than 71.0% protein, calculated on the dried basis. 

Numbers of residues are given per 23,800 gm for bovine trypsinogen. They are given per 24,900 gm for porcine trypsinogen and also per 100 gm, since the molecular weight of this protein calculated from chemical analysis alone is still preliminary. Preliminary value estimated from chemical analysis. 

Figure 3. Correlation of Scores on Propsearch or ExPASy with Average Error of Analysis. The score given by Propsearch (graph on left) or ExPASy (graph on right) for tpis rabit was plotted against the average error for that analysis of the protein. Calculated mol % data for the query protein were submitted to search programs without calibration standard (if any). Proteins ranked as number 1 A, rabbit tpis , tpis from species other than rabbit and o, other protein.

Ribosomes from Escherichia coli Asymmetrical Separation of ribosomes, their subunits, and t-RNA/low-MW protein mixture in samples collected at different protein production phases and in the presence of antibiotics, specific genes, and proteins calculation of a ribosome number per cell and a ribosome fraction using peak area [6]... 

A less expensive technique often used for protein calculations is the accessible surface area method that supposes that the contribution of each atom to the total solvation free energy of the system is proportional to the solvent accessible surface area of the atom [81, 82],... 

The molar ratio of bound flavin to protein (calculation based on the molecular weight of luciferase) was found to be about 0.75. This is not far from the expected ratio of 1 1 if one takes into account the fact that the preparation was only about 80% pure as judged by its spectral properties (Meighen and Hastings, 1971 Baldwin et al., 1975). 

Since a variation from these standard angles is found for jS turns in proteins, calculations were also done on structures having different (, i/()2 and (,. Analysis of the structural data on 38 nonhomologous pro-... 

Figure 5 RADACK applied to a DNA-binding protein. Calculated relative probabilities of reaction of OH radicals with the amino-acids of lactose repressor headpiece along the free irradiated headpiece (structure extracted from ILQCentry from PDB) (black) and along the headpiece Irradiated In complex with DNA (structure extracted from ICJG entry from PDB) (red).

Average Percentage of Amino Acids in Fish Proteins (Calculated to 16% N)... 

Q.27.12 Given the following rates of fluorescence and absorption of several different proteins, calculate the following quantum yields, (a) Fluorescence Rate 50 s , Absorption Rate 60 s (b) Fluorescence Rate 33 s . Absorption Rate 42 s (c) Fluorescence Rate 112 s . Absorption Rate ... 

The optimum dosage levels are also affected by the pH level. Although lysozyme recovery was nearly quantitative, the polymer requirements decreased with the net charge on the protein. Calculations, summarized in Table 3, indicate that for the precipitation of lysozyme at pH 4.2, a nearly electrostatically neutral complex is formed. Note that the extent of charge neutralization is reduced by increased ionic strength, and that this effect is most pronounced for proteins with low net charges. 

Molecular and Cellular Proteomics. Bethesda, MD American Society for Biochemistry and Molecular Biology. Monthly. ISSN 1535-9476. Scope includes structural and functional properties of proteins and their expression, developmental time courses of the organism, how the presence or absence of proteins affects biological responses and how the interaction of proteins with germane cellular partners allows them to function, and advances in methodology, array technologies, changes in expression of the proteins, calculations and/or predictions, and aspects of bioinformatics that address needs in proteomics. 

The excluded volume (per mol) of the globular protein calculated above is about 9 times the molar volume. This compares well with the case of spherical particles for which the excluded volume equals eight times the particle volume. 

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