Shoemaker K R, Kim P S, York E J, Stewart J M, Baldwin R L
Nature. 1987;326(6113):563-7. doi: 10.1038/326563a0.
Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm-Bragg model for alpha-helix formation.
带电基团在分离的C肽(核糖核酸酶A的1-13位残基)在水溶液中形成的螺旋稳定性中起着关键作用。一种带电基团效应可能源于螺旋两端的带电残基与螺旋偶极之间的相互作用。我们在此报告,对C肽类似物的研究支持螺旋偶极模型,并为Zimm-Braggα-螺旋形成模型中未包含的静电相互作用的重要性提供了进一步证据。