Folding, aggregation and molecular recognition in peptides

• Published in: Acta crystallographica. Section B, Structural science Vol. 48 ( Pt 4); p. 341
• Main Author: Karle, I L
• Format: Journal Article
• Language: English
• Published: United States 01-08-1992
• Subjects: Amino Acid Sequence; Aminoisobutyric Acids; Crystallization; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Molecular Structure; Peptides - chemistry; Protein Conformation; X-Ray Diffraction
• ISSN: 0108-7681
• DOI: 10.1107/S0108768192000673

In past years, most of the X-ray structure determinations of oligopeptides were for cyclic peptides or for short linear peptides. Longer peptides usually presented many difficulties in obtaining suitable crystals since the molecules are intrinsically very flexible. More recently, it has been appreciated that the aminoisobutyric acid residue (Aib), which occurs naturally in many peptides of microbial origin, initiates helix folding. Several score of 7- to 15-residue linear peptides containing Aib have been synthesized, crystallized and had their structures determined to high resolution. Many of the peptide structures have been determined in more than one crystalline form. These peptide structures have yielded a plethora of information on types of helices, modes of hydration, water penetration into helical backbones, helices bent by Pro residues, parallel and antiparallel association of helices, effects of Leu residues on association of peptides, an example of a zipper assembly by side chains, and an example of a possible ion channel with a gating mechanism.