Abstract
Since the first and the last residues of a protein have peculiar properties, unique amongst all residues, they have been analyzed repeatedly during the last decades. In this brief review, I try to summarize, besides the biochemical roles, the five features that have attracted most attention: (i) the Euclidean distance between the N- and C-termini and its relevance to protein folding, (ii) the reason why the termini are solvent exposed, (iii) the backbone conformation of the termini, (iv) the amino acid composition of the termini, and (v) the role of the termini in protein crystallization. Each of these five issues, which deserve attention nowadays thanks to the availability of massive amounts of data, is accompanied by my personal outlook of the research in the field.
Keywords: Amino acid composition, protein crystallization, protein structure, protein termini, secondary structure, solvent exposure.
Current Protein & Peptide Science
Title:Protein Termini
Volume: 18 Issue: 3
Author(s): Oliviero Carugo
Affiliation:
Keywords: Amino acid composition, protein crystallization, protein structure, protein termini, secondary structure, solvent exposure.
Abstract: Since the first and the last residues of a protein have peculiar properties, unique amongst all residues, they have been analyzed repeatedly during the last decades. In this brief review, I try to summarize, besides the biochemical roles, the five features that have attracted most attention: (i) the Euclidean distance between the N- and C-termini and its relevance to protein folding, (ii) the reason why the termini are solvent exposed, (iii) the backbone conformation of the termini, (iv) the amino acid composition of the termini, and (v) the role of the termini in protein crystallization. Each of these five issues, which deserve attention nowadays thanks to the availability of massive amounts of data, is accompanied by my personal outlook of the research in the field.
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Cite this article as:
Carugo Oliviero, Protein Termini, Current Protein & Peptide Science 2017; 18 (3) . https://dx.doi.org/10.2174/1389203717666160822121527
DOI https://dx.doi.org/10.2174/1389203717666160822121527 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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