Abstract:
:In the present paper we describe the synthesis, purification, and single crystal x-ray analysis of the cyclic pentapeptide cyclo-(Pro-Phe-Phe-beta-Ala-beta-Ala). This compound crystallizes in the orthorhombic space group P2I2I2I from methanol and adopts in the solid state an unusual conformation characterized by a cis beta-Ala5-Pro1 peptide bond and by an intramolecular hydrogen bond stabilizing a C11-and a C12-ring structure. The C11 structure contains the Phe3 and the beta-Ala4 at the corner position of the turn; it is the first observation of a type II beta-turn enlargement due to the insertion of an extra methylene group of the beta-alanine residue. The rest of the molecule participates in a newly characterized C12-ring structure, which incorporates a beta-Ala residue at position i of the turn.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Lombardi A,Saviano M,Nastri F,Maglio O,Mazzeo M,Pedone C,Isernia C,Pavone Vdoi
10.1002/bip.360380602subject
Has Abstractpub_date
1996-06-01 00:00:00pages
683-91issue
6eissn
0006-3525issn
1097-0282journal_volume
38pub_type
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