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Edman degradation

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A method of sequencing amino acids in a peptide. The amino-terminal residue is labelled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues.

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degradación de Edman

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A method of sequencing amino acids in a peptide.
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Método de secuenciación de aminoácidos en un péptido.
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A key feature is repetitive N-terminal identification using the Edman degradation.
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The chain-shortened peptide is then automatically resubmitted to another round of Edman degradation.
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The N-terminals were determined by the Edman degradation method.
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Each Edman degradation cleaves the N-terminal amino acid and forms its phenylthiohydantoin derivative.
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The resulting smaller fragments are then sequenced by Edman degradation.
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We’ll discuss one of these—the Edman degradation—in Section 27.13.
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(b) Explain why the Edman degradation is usually preferred over the Sanger method.
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The Edman degradation is based on the chemistry shown in Mechanism 27.3.
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H Edman degradation: Method for determining the N-terminal amino acid of a peptide or protein.
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An automated instrument known as a sequenator allows about 50 successive Edman degradations to be performed.
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In theory, Edman degradations could sequence a peptide of any length.
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Figure 3.18 Edman degradation procedure.
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Edman degradation gave PTH-Ala. 2.
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Also in common use is a chemical method of peptide sequencing called the Edman degradation.
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These fragments can then be separated and sequenced by Edman degradation.
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The remainder of the peptide (formed in step 2) can be isolated and subjected to a second Edman degradation.
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Protein sequence can be determined by Edman degradation, in which the N-terminal residues are hydrolyzed from the chain one at a time, derivatized, and then identified.
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The amino acid sequence of the protein was analyzed by Edman degradation and then used to construct a cDNA library which could be used to clone the channel protein.
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The plasminogens were purified by the same methods: affinity and ion exchange chromatographies, furthermore both plasminogen were activated by human urokinase and the N-terminals sequence perform by the Edman's degradation's method.
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The resultant smaller peptides can be chromatographically separated and subjected to Edman degradation sequencing reactions.
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Edman degradation, developed by Pehr Edman, is a method of sequencing amino acids in a peptide.
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Due to the limitations of the Edman degradation technique, peptides longer than around 50 residues can not be sequenced completely.
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The combination of techniques such as automated Edman degradation and de novo sequencing by MALDI-TOF MS allowed the establishment of its primary structure.
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Edman degradation using a protein sequenator is the second method, which is most useful if the N-terminus of a protein needs to be characterized.
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By a peptidomic approach, integrating molecular cloning, Edman degradation sequencing and tandem mass spectrometry, a new family of antimicrobial peptides has been identified in Cruziohyla calcarifer.
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