Amino acids sequence in peptides

E3. Edman, P., Method for determination of the amino acid sequence in peptides. Acta Chem. Scand. 4, 283-293 (1950). 

As of this writing, 50 years have passed since Pehr Edman published his first note on chemical degradation of peptide chains, A Method for the Determination of the Amino Acid Sequence in Peptides. As testament to the continuing relevance of this technique, the following job announcement was recently posted. 

By definition, a structural subunit is repeated periodically in an oligomer or in a polymer inducing a corresponding periodicity of fragmentation in the mass spectrometer. If a fragmentation series due to such a periodicity of structure is detectable, an analysis of the sequence of monomers in oligomers is possible. This may be discussed in the case of amino acid sequencing in peptides ... 

K. Biemann, F. Gapp, J. Seibl, Application of mass spectrometry to stracture problems I, Amino acid sequence in peptides. J. Amer. Chem. Soc. 81 2274-2275 (1959)... 

P. Edman, Determination of the amino acid sequence in peptides. Arch. Biochem. 22 475-476 (1949) also Method for the determination of the amino acid sequence in peptides. Acta Chem. Scand. 4 283-293 (1950) Stepwise degradation of peptides via phenylthiohydantoins. Acta Chem. Scand. 7 700-701 (1953)... 

Used (with octadecanoic acid) for amino acid sequencing in peptides. Cryst. (pet. ether). Mp 62-63°. 

Constit. of most vegetable and animal fats. Acid and derivatives widely used as additives to industrial preparations. Used as EtOH soln. for nephelometric detn. of Ca. Used (with heptadecanoic acid) for amino acid sequencing in peptides. Leaflets. Sol. EtOH, C Hg, CHCI3 si. sol. H2O. Mp 69.7°. Bp5 213°. 

Eng, J. K. McCormack, A. L. Yates, J. R. An approach to correlate tandem mass spectra data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994,5, 976-989. 

Because of their known specificity, these enzymes, especially trypsin and chymotrypsin, have been widely utilized in helping to determine the amino acid sequences of peptides (see Section 13.7). Hydrolysis using these... 

Protein biosynthesis involves the translation of the information contained in a base sequence in a specific mRNA into the synthesis of an amino acid sequence, or peptide. 

Messenger RNA Translation Predict the amino acid sequences of peptides formed by ribosomes in response to the following mRNA sequences, assuming that the reading frame begins with the first three bases in each sequence. 

When an unknown peptide containing five amino acids is treated with an enzyme that hydrolyzes only the serine-leucine peptide bond, the fragments Leu—Cys, Ser, Leu— Ser are formed. What was the original amino acid sequence in the peptide ... 

Protein biosynthesis is the process by which the message carried in the base sequence is transformed into an amino acid sequence in a peptide or protein. 

Aside from gastrointestinal and renal metabolism, the liver may also contribute substantially to the metabolism of peptide and protein drugs. Proteolysis usually starts with endopeptidases that attack in the middle part of the protein, and the resulting oligopeptides are then further degraded by exopeptidases. The ultimate metabolites of proteins, amino acids and dipeptides, are finally reutilized in the endogenous amino acid pool. The rate of hepatic metabolism is largely dependent on specific amino acid sequences in the protein. 

Peptides and proteins exhibit distinct species specificity with regard to structure and activity. Peptides and proteins with identical physiological function may have different amino acid sequences in different species, and may have no activity or be even immunogenic if used in a different species. 

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