Crystal structure of a synthetic cyclodecapeptide for template-assembled synthetic protein design

Chembiochem. 2001 Jun 1;2(6):432-7. doi: 10.1002/1439-7633(20010601)2:6<432::AID-CBIC432>3.0.CO;2-6.

Abstract

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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Structure
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / chemistry*
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • Peptides, Cyclic