Proteins large

Laser desorption methods are particularly useful for substances of high mass such as natural and synthetic polymers. Glycosides, proteins, large peptides, enzymes, paints, ceramics, bone, and large... 

Rudenko, G., et al. (2003). MADTy phasing the extracellular domain of the LDL receptor a medium-sized protein, large timgsten clusters and multiple non-isomorphous crystals. Acta Crystallogr. D 59,1978-1986. 

Proteins—Large molecules produced by living organisms, composed of one or more chains of amino acids. These may be modified by the addition of sugars or other chemical substances. 

Incompatibility of some proteins (large, hydrophobic proteins) with the first-dimension IEF step... 

Because mD N is proportional to the number of groups in the protein, large proteins are more sensitive to solvent denaturation than small ones. It is a common mistake to attribute resistance to solvent denaturation of small proteins to high stability in fact, it is an inherent characteristic of a small change in surface area on denaturation. Also, proteins that are elongated have higher solvent exposure in the native state and correspondingly lower values of mD N. 

I The most important properties of a protein are deter-f mined by the sequence of amino acids in the polypeptide chain. This sequence is called the primary structure of the protein. We know the sequences for thousands of peptides and proteins, largely through the use of methods developed in Fred Sanger s laboratory and first used to determine the sequence of the peptide hormone insulin in 1953. Knowledge of the amino acid sequence is extremely useful in a number of ways (1) it permits comparisons between normal and mutant proteins (see chapter 5) (2) it permits comparisons between comparable proteins in different species and thereby has been instrumental in positioning different organisms on the evolutionary tree (see fig. 1.24) (3) finally and most important, it is a vital piece of information for determining the three-dimensional structure of the protein. 

Fractionation with organic solvents is mainly done to remove proteins, large peptides, and non-proteinaceous material such as fat. In a method developed by Harwalkar and Elliott (1971) and adopted by Lemieux et al. (1990), Puchades et al. (1990), and Visser et al. (1983), freeze-dried samples of cheese were extracted using methanol (to precipitate large peptides and proteins), chloroform (to remove fat), and water. The final extract... 

As the ocular muscle enters the orbit, its appearance changes dramatically. Most of the muscle cytoplasm is lost, contractile proteins largely disappear, and mitochondrial abundance increases dramatically, to assume up to about two-thirds of cell volume. Another striking feature of heater organ cells is the development of an elaborate membrane wrapping around the mitochondria (figure 7.32). This extensively developed membrane system is derived from the sarcoplasmic reticular membranes. The high densities of ion pumps in the... 

Proteins largely and extensively exist in all kinds of living beings, constructing their bodies and also acting as information carriers as well as recognition... 

Mass loadability of SPE and RAM columns play a key role in executing the sample clean-up. It is advisable to work below the overload regime of the column. Otherwise, displacement effects and other phenomena such as secondary interaction by adsorbed species might take place, which will lead to nonrepro-ducible results. This last statement is particularly important when the task is to monitor medium-to-low-abundance proteins large sample volumes in the milliliter range are therefore usually applied. 

Rischel, C., Spiedel, D., Ridge, J. P., Jones, M. R., Breton, J., Lambry, J. C., Martin, J. L., and Vos, M. H., 1998, Low-frequency vibrational modes in proteins large frequency-shifts induced by point-mutations in ftie protein-cofactor matrix of bacterial reaction centers. Proc. Natl. Acad. Sci. USA, 95 12306nl2311. 

ART Mono-ADP-ribosyltransferase family of proteins, large group of A-B toxins... 

It should be stressed that proteins are more than just the sum of the amino acids that comprise them. Surprises abound when predicting the chemical modification behavior of a particular protein, largely because of the complex interplay between the individual functional groups and the local environments in which they reside. Nevertheless, the first step to understanding the chemical behavior of proteins is to characterize the reactive properties of the individual side chain groups. The following sections describe these aspects, with an emphasis on the chemical techniques that are commonly used to modify these residues for applications in chemical biology. 

Because carbohydrate utilization is impaired, a lack of insulin leads to the uncontrolled breakdown of lipids and proteins. Large amounts of acetyl CoA are then produced by P-oxidation. However, much of the acetyl CoA cannot enter the citric acid cycle, because there is insufficient oxaloacetate for the condensation step. Recall that mammals can synthesize oxaloacetate from pyruvate, a product of glycolysis, but not from acetyl CoA instead, they generate ketone bodies. A striking feature of diabetes is the shift in fuel usage from carbohydrates to fats glucose, more abundant than ever, is spurned. In high concentrations, ketone bodies overwhelm the kidney s capacity to maintain acid-base balance. The untreated diabetic can go into a coma because of a lowered blood pH level and dehydration. 

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