title: Protein Termini.
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.
authors.affiliation: Department of Chemistry, University of Pavia, viale Taramelli 12, I-27100 Pavia, Italy and Department of Structural and Computational Biology, Vienna University, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
authors.forename: Oliviero
authors.initials: O
authors.lastname: Carugo
mesh_terms: D000596:Amino Acids / Q000032:analysis; D003460:Crystallization; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry
chemical_list: D000596:Amino Acids; D011506:Proteins; D012997:Solvents
keywords: Amino acid composition; protein crystallization; protein structure; protein termini; secondary structure; solvent
  exposure