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Citation: Gao Feng, Sha Yin-Lin, Qiu Yang, Wang Yue-Feng, Li Yin-Ling, Lai Lu-Hua, Wu Hou-Ming. Solution Conformation Study on a β-turn Forming Peptide[J]. Acta Physico-Chimica Sinica, ;2001, 17(07): 619-621. doi: 10.3866/PKU.WHXB20010709 shu

Solution Conformation Study on a β-turn Forming Peptide

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 Date: 12 February 2001
Available Online: 15 July 2001

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.
- β-turn;CD;FT-IR;NMR;Peptide
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