Crystal structure of a synthetic cyclodecapeptide for template-assembled synthetic protein design.
The structural prototype of a new generation of regioselectively addressable functionalized templates (RAFTs) for use in protein de novo design has been synthesized and crystallized. The structure of the aromatically substituted cyclodecapeptide was determined by X-ray diffraction; it consists of an antiparallel beta sheet spanned by heterochirally induced type IIprime prime or minute beta turns, similar to that observed in gramicidin S. The three-dimensional structure of the artificial template was also examined by an NMR spectroscopic analysis in solution and shown to be compatible with a beta-sheet plane suitable for accommodating secondary functional peptide fragments for the synthesis of template-assembled synthetic proteins (TASPs).
Peluso
S
S
Institute of Organic Chemistry, University of Lausanne, BCH-Dorigny, 1015 Lausanne-Dorigny, Switzerland.
Rückle
T
T
Lehmann
C
C
Mutter
M
M
Peggion
C
C
Crisma
M
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D010456:Peptides, Cyclic