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1篇 您的检索式:作者名="Daniel P.Miller"
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1Reliable folding of hybrid tetrapeptides into shortβ-hairpins显示文摘Five hybrid tetrapeptides,each consisting a central dipeptide segment ofα-amino acid residues flanked by two aromaticγ-amino acid residues,are found to fold into well-definedβ-hairpin conformations as shown by NMR,computational study,and X-ray structures.The turn loop of thisβ-hairpin motif accommodates different two-residueα-amino acid sequences from the highly flexible Gly-Gly,to the more restricted D-Pro-Gly.The presence ofα-amino acid side chains enhances the stabilities of theβ-hairpins with the exception of D-Pro-Gly-which results in destabilization.Based on this hairpin/turn motif,a variety of different dipeptide sequences ofα-amino acids which rarely occur inβ-turns can be introduced and presented as two-residue loops.Xue-Yi Sun Yulong Zhong Yao-Hua Li Daniel P.Miller Sagar Buttan Xiang-Xiang Wu Yukun Zhang Quan Tang Hong-Wei Tan Jin Zhu Rui Liu Eva Zurek Zhong-Lin Lu Bing Gong 2022Chinese Chemical Letters2022,33,1:0
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