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Proteins evaluation

The treatment described above (which was introduced in Ref. 1) is much simpler than the standard treatment (which uses internal coordinates b, 0, large molecules or small proteins, evaluating the second derivative matrix F numerically, using analytical first derivatives. [Pg.118]

Figure 2-7. Origins of the increased O2 binding energy in IPNS when the protein is included in an ONIOM model. (A) A comparison of the optimized geometries from an active-site model (silver) and an ONIOM protein model (dark grey), show that the artificial structural relaxation of the active-site model is more pronounced for the reactant state than for the product state. (B) Contributions to O2 binding from the surrounding protein, evaluated only at the MM level (Adapted from Lundberg and Morokuma [26], Reprinted with permission. Copyright 2007 American Chemical Society.)... Figure 2-7. Origins of the increased O2 binding energy in IPNS when the protein is included in an ONIOM model. (A) A comparison of the optimized geometries from an active-site model (silver) and an ONIOM protein model (dark grey), show that the artificial structural relaxation of the active-site model is more pronounced for the reactant state than for the product state. (B) Contributions to O2 binding from the surrounding protein, evaluated only at the MM level (Adapted from Lundberg and Morokuma [26], Reprinted with permission. Copyright 2007 American Chemical Society.)...
Yoda T, Sugita Y, Okamoto Y (2004) Secondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulations. Chem Phys 307 269... [Pg.169]

Siegel, N., Stadler, J., Tilbury, L. and Smith, D. (2007) PEGylated proteins evaluation of their safety in the absence of definitive metabolism studies. Drug Metab. Dispos., 35 (1), 9-16. [Pg.277]

Young, V.R. and Pellett, P.L. 1991. Protein evaluation, amino acid scoring and the Food and Drug Administration s proposed food labeling regulations. J. Nutr. 121 145-150. [Pg.139]

Pearce, K.N. and Kinsella, J.E. 1978. Emulsifying properties of proteins Evaluation of a turbidimetric technique. J. Agric. Food Chem. 26 7lb-723. [Pg.293]

RB Ashworth. Amino acid analysis for meat protein evaluation. J Assoc Off Anal Chem 70 80-85, 1987. [Pg.89]

R.D. Waniska and J.E. Ninsella, Foaming properties of proteins evaluation of a column aeration apparatus using ovalbumin, J. Food Sci. 44 (1979) 1398-1402. [Pg.282]

Gillis D, Rooman M (1996) Stability changes upon mutation of solvent-acessible residues in protein evaluated by database-derived potentials J Mol Biol, 257 1112-1126... [Pg.328]

Brass LF, LAPOSATA M, Banga HS, RTTTENHOUSE SE. Regulation of the phosphoinositide hydrolysis pathway in thrombin-stimulated platelets by pertussis toxin-sensitive guanine nudeotide-binding protein Evaluation of its contribution to platdet activation and comparisms with the adenylate cydase inhibitory protein, Gl. JBiol Chem 261 16838-16847,1986. [Pg.219]

BRASS LF, LAPOSATA M, BANGA HS, RTITENHOUSE SE (1986) Relation of the phosjAoinositide hydrolysis pathway in thrombin-stimulated platelets by a pertussis toxin-senative guanine nucleotide-binding protein. Evaluation of its contribution to platelet activation and comparisons with the adenylate cyclase inhibitory protein, Gi. Journal of Biological Chemistry, 261,16838-16847. [Pg.248]

Forsum, E. Goranzon, H. Rundgren, M. Thilen, M. Hambraeus, L. Protein evaluation of mixed diets. Comparative study in man and in the pig and rat of vegetable-animal and vegetable protein diets. Ann. Nutr. Metab. 1981, 25 (3), 137-150. [Pg.2827]

Oppenheimer, J. H., Squef, R., Surks, M. I., and Hauer, H., Binding of thyroxine by serum proteins evaluated by equilibrium dialysis and electrophoretic techniques Alterations in non-thyroidal illness. J. Clin. Invest. 42, 1769-1782 (1963). [Pg.421]

Cozzini, P., Fornabaio, M., Marabotti, A., Abraham, D.J., Kellogg, G.E., and MozzareDi, A. (2004) Free energy of ligand binding to protein evaluation of the contribution of water molecules by computational methods. Current Medicinal Chemistry, 11, 3093—3118. [Pg.283]

Rama, P. B., Norton, H. W., and Johnson, C. (1964). The amino acid composition and nutritive value of proteins. V. Amino acid requirements as a pattern for protein evaluation. /. Nutr. 82, 88-92. [Pg.312]

The Protein Digestibility Corrected Amino Acid Score (PDCAAS) is superior to other methods for evaluating the protein quality of food proteins for humans because it measures the quality of a protein based on the amino acid requirements of a 2-5 year old child (the most demanding age group), adjusted for digestibility [120]. It has replaced the Protein Evaluation Ratio (PER). [Pg.91]

Bodwell, C.E., Carpenter, K.J., and McDonough, F.E. A coUahorative study of methods of protein evaluation introductory paper. Plant Foods Hum. Nutr. 39 3-11,1989. [Pg.99]

Chapter 13 examines the protein value of foods and the measures used to quantify protein supply to both monogastric and ruminant animals, which, again, differ as a consequence of their digestive systems. Details are given of the current protein evaluation systems used in the UK. [Pg.235]

Table 13.10 Comparison of estimates of the efficiency of utilisation of truly digested true protein made in some protein evaluation systems for ruminants... Table 13.10 Comparison of estimates of the efficiency of utilisation of truly digested true protein made in some protein evaluation systems for ruminants...
Assays of available amino acids may be made by measuring the liveweight gain or food conversion efficiency of animals given the intact protein as a supplement to a diet deficient in a particular essential amino acid. Certain microorganisms have amino acid requirements similar to those of higher animals and have been used for protein evaluation. [Pg.338]

Maggi, V. 2001. Microbial PS149B1 Binary Insecticidal Crystal Protein, Pollen Expressing PS149B1 Binary Insecticidal Crystal Protein, and Individual PS149B1 14 kDa and 44 kDa Insecticidal Crystal Proteins Evaluation of Dietary Exposure on Honeybee Development Lab Project Number CAR 149-00. Unpublished study prepared by California Agricultural Research, Inc. 58 p. OPPTS 885.4380 ... [Pg.295]


See other pages where Proteins evaluation is mentioned: [Pg.123]    [Pg.14]    [Pg.1008]    [Pg.85]    [Pg.642]    [Pg.325]    [Pg.326]    [Pg.148]    [Pg.153]    [Pg.154]    [Pg.403]    [Pg.64]    [Pg.904]    [Pg.380]    [Pg.405]    [Pg.405]    [Pg.28]    [Pg.287]    [Pg.288]    [Pg.289]   
See also in sourсe #XX -- [ Pg.372 , Pg.373 , Pg.374 ]

See also in sourсe #XX -- [ Pg.372 , Pg.373 , Pg.374 ]

See also in sourсe #XX -- [ Pg.876 ]




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Biological Evaluation of Proteins

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Evaluating protein models

Evaluation of foods protein

Evaluations of Novel Canine Renal Protein Biomarker Performance

Example Evaluation of Protein Models

Horse protein evaluation

Protein Volume Evaluation (PROVE)

Protein affinity chromatography evaluation

Protein folding scoring function evaluation

Protein structure evaluation

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Sequencing, proteins data evaluation

Step 6 Evaluating Protein Models

The Field Evaluation of Transgenic Crops Engineered to Produce Recombinant Proteins

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