引用本文:
Li Ping LIU, Zhi Dong XIE, Bing Lin HE. EFFECT OF AMPHIPHILIC α-HELICES OF PEPTIDES ON THEIR BINDING TO CALMODULIN[J]. Chinese Chemical Letters,
1995, 6(2): 117-120.
Citation: Li Ping LIU, Zhi Dong XIE, Bing Lin HE. EFFECT OF AMPHIPHILIC α-HELICES OF PEPTIDES ON THEIR BINDING TO CALMODULIN[J]. Chinese Chemical Letters, 1995, 6(2): 117-120.
Citation: Li Ping LIU, Zhi Dong XIE, Bing Lin HE. EFFECT OF AMPHIPHILIC α-HELICES OF PEPTIDES ON THEIR BINDING TO CALMODULIN[J]. Chinese Chemical Letters, 1995, 6(2): 117-120.
EFFECT OF AMPHIPHILIC α-HELICES OF PEPTIDES ON THEIR BINDING TO CALMODULIN
摘要:
Melittin is a small basic peptide which has a high affinity for calmodulin(CaM).In a previous paper,the authors have demonstrated that the deletion peptide Mel(12~25),that is,Mel15 has almost the same binding activity as the intact native peptide(1).In this study,three analogues of Mel15 were synthesized,the role of amphiphilic α-helix of peptides on their binding to CaM were studied.According to the calculation of hydrophobic moment and the analysis of the secondary structure,we proposed that the role of amphiphilic structure is not absolute,since the dissociation constants for the binding of different analogs to CaM bear no predictable relation to the calculated hydrophobic moment and the average hydrophobicity
English
EFFECT OF AMPHIPHILIC α-HELICES OF PEPTIDES ON THEIR BINDING TO CALMODULIN
Abstract:
Melittin is a small basic peptide which has a high affinity for calmodulin(CaM).In a previous paper,the authors have demonstrated that the deletion peptide Mel(12~25),that is,Mel15 has almost the same binding activity as the intact native peptide(1).In this study,three analogues of Mel15 were synthesized,the role of amphiphilic α-helix of peptides on their binding to CaM were studied.According to the calculation of hydrophobic moment and the analysis of the secondary structure,we proposed that the role of amphiphilic structure is not absolute,since the dissociation constants for the binding of different analogs to CaM bear no predictable relation to the calculated hydrophobic moment and the average hydrophobicity
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