Acta Phys. -Chim. Sin. ›› 2001, Vol. 17 ›› Issue (07): 619-621.doi: 10.3866/PKU.WHXB20010709

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Solution Conformation Study on a β-turn Forming Peptide

Gao Feng;Sha Yin-Lin;Qiu Yang;Wang Yue-Feng;Li Yin-Ling;Lai Lu-Hua;Wu Hou-Ming   

  1. Institute of Physical Chemistry,College of Chemistry and Molecular Engineering ,State Key Laboratory for Structural Chemistry of Unstable & Stable Species,Pek ing University,Beijing 100871;Department of Biophysics,The School of Basic Medical Sciences,Peking University,Beijing 100083;Institute of Organic Chemis try,Chinese Academy of Sciences,Shanghai 200032
  • Received:2001-02-12 Revised:2001-03-15 Published:2001-07-15
  • Contact: Sha Yin-Lin

Abstract: The model six-residue linear peptide AAGDYY-NH2 from TEM-1 β-lact amase inhibitor protein and BLIP was predicted to adopt a β-turn conformation and synthesized in order to elucidate the mechanism of β-turn formation and s tability.Its structural preferences in solution were comprehensively characteriz ed using CD (circular dichroism),FT-IR and 1H-NMR spectroscopy.The set of obse rved short- and medium-range NOEs,the restrained molecular dynamics simulation ,CD and FT-IR spectroscopy were consistent with the formation of β-turn in so lution by the model peptide.The results implicate β-turn playing an important role in the process of protein folding.

Key words: β-turn, CD, FT-IR, NMR, Peptide