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A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins

Proteins, v.80 no.4, 2012년, pp.977 - 990  

Oh, Kwang‐Im (Department of Chemistry, Korea University, Seoul 136‐) ,  Lee, Kyung‐Koo (701, Korea) ,  Park, Eun‐Kyung (Department of Chemistry, Korea University, Seoul 136‐) ,  Jung, Youngae (701, Korea) ,  Hwang, Geum‐Sook (Department of Chemistry, Korea University, Seoul 136‐) ,  Cho, Minhaeng (701, Korea)

Abstract AI-Helper 아이콘AI-Helper

AbstractDespite prolonged scientific efforts to elucidate the intrinsic peptide backbone preferences of amino‐acids based on understanding of intermolecular forces, many open questions remain, particularly concerning neighboring peptide interaction effects on the backbone conformational distri...

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참고문헌 (55)

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