Serine structural formula

Strategy Write the condensation reaction that takes place between glycine and serine. To do this, start with the structural formulas of the two amino acids, glycine at the left, serine at the right. In each case, put the NH2 group at the left, the COOH group at the right. Condense out a water molecule what is left is the structural formula of Gly-Ser. 

Give the structural formula of two different dipeptides formed between arginine and serine. 

Using partial structural formulas, describe the reactions by which serine and methionine react to form N-formy I methionine needed for protein synthesis. 

Chemical Name DL-Serine 2-[(2,3,4-trihydroxyphenyl)methyl]hydrazide Common Name -Structural Formula ... 

The structural formulas of phosphatidyl choline and the other principal phosphoglycerides—namely, phosphatidyl ethanolamine, phosphatidyl serine, phosphatidyl inositol, and diphosphatidyl glycerol—are given in Figure 12.5. 

Structural formulae of L-alanyl-L-serine (ala-ser) and L-alanyl-L-histidine (ala-his) in their zwitterionic representation, and proposed structures of the predominant vanadate complexes. For the ala-ser complexes, see also the speciation diagram in Figure 2.16. 

Exercise 25.53(b) asks for the number of and abbreviations for the tripeptides that can be made from the amino adds serine and phenylalanine. Using information from the Proteins and Amino Acids movie eChapter 25.9) and the table of structural formulas of amino adds in Figure 25.21, draw the structures for each of the tripeptides in your answer to Exercise 25.53(b). 

Write a complete structural formula and an abbreviated formula for the tripeptide formed from tyrosine, serine, and phenylalanine in which the C-terminal residue is serine and the N-terminal residue is phenylalanine. 

Following are two structural formulas for (S)-serine, one of the building blocks of proteins (Chapter 27). 

Structural formula A contains both an amino group (a base) and a carboxyl group (an acid). Proton transfer from the stronger acid (—COOH) to the stronger base (—NHj) gives an internal salt therefore, B is the better representation for (S)-serine. Within the field of amino acid chemistry, the internal salt represented by B is called... 

The amino acid serine has the condensed structural formula ... 

Write the structural formulas of all possible tripeptides with the composition of two glycines and one serine. (See the structural formulas in Table 25.2.)... 

Draw the condensed structural formula and give the abbreviations for serine, serine (R = —CH2—OH)... 

Write the structural formula of the two amino acids side by side. Put glycine on the left with the NH2 group on the left and the COOH group on the right. Put the serine group on the right in a similar fashion. 

Lecithins and cephalins are two types of glycerophospholipids that are particularly abundant in brain and nerve tissues as well as in egg yolks, wheat germ, and yeast. Lecithins contain choline, and cephalins usually contain ethanolamine and sometimes serine. In the following structural formulas, the fatty acid that is used as an example is palmitic acid ... 

Draw the condensed structural formula for the cephaUn that contains two stearic acids on the first and second carbon atoms, with serine as the ionized amino alcohol. 

Fig. 7.5. General formula summarizing the structural and stereochemical requirements, which an ester should meet to fit into the active site of pig liver esterase. A nucleophilic attack by the serine OH group seemingly occurs from this side B no or only small substituents allowed here C groups of small to medium size allowed in this area D space allowed in these areas for carbon chains, with polar substituents (e.g., another ester group) preferred in the upper part ...

A particularly striking feature of the simplified formula of the tobacco mosaic virus (Fig. 14) is the stereotype repetition of several simple structures (combinations UI, LS, AF) which in fact represent the cornerstones of the entire molecule. A phenomenon deserving special interest (apart from a number of symmetrical sequences occurring along the whole chain) is the symmetrical arrangement of the dipeptides of the hydroxyamino acid residues at both terminals of the polypeptide chain. This relative concentration of the serine residues at the ends of the tobacco mosaic virus protein chain has been pointed out by Anderer et al. (1960) as a possible example of nonrandomness. 

Give the general formula for an amino acid. Some amino acids are labeled hydrophilic and some are labeled hydrophobic. What do these terms refer to Aqueous solutions of amino acids are buffered solutions. Explain. Most of the amino acids in Fig. 22.18 are optically active. Explain. What is a peptide bond Show how glycine, serine, and alanine react to form a tripeptide. What is a protein, and what are the monomers in proteins Distinguish between the primary, secondary, and tertiary structures of a protein. Give examples of the types of forces that maintain each type of structure. Describe how denaturation affects the function of a protein. 

The side chains of proteins can undergo post-translational modification in the course of thermal processes. The reaction can also result in the formation of protein cross-links. A known reaction which mainly proceeds in the absence of carbohydrates, for example, is the formation of dehydroalanine from serine, cysteine or serine phosphate by the elimination of H2O, H2S or phosphate. The dehydroalanine can then lead to protein cross-links with the nucleophilic side chains of lysine or cysteine (cf. 1.4.4.11). In the presence of carbohydrates or their degradation products, especially the side chains of lysine and arginine are subject to modification, which is accompanied by a reduction in the nutritional value of the proteins. The structures of important lysine modifications are summarized in Formula 4.95. The best known compounds are the Amadori product -fructoselysine and furosine, which can be formed from the former compound via the intermediate 4-deoxyosone (Formula 4.96). To detect of the extent of heat treatment, e. g., in the case of heat treated milk products, furosine is released by acid hydrolysis of the proteins and quantitatively determined by amino acid analysis. In this process, all the intermediates which lead to furosine are degraded and an unknown portion of already existing furosine is destroyed. Therefore, the hydrolysis must occur under standardized conditions or preferably by using enzymes. Examples showing the concentrations of furosine in food are presented in Table 4.13. 

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