Fiori W R, Millhauser G L
Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.
Biopolymers. 1995;37(4):243-50. doi: 10.1002/bip.360370403.
Over the last several years we have used spin labeling as a means for exploring the structure of helical peptides. Two nitroxide labels are engineered into a peptide sequence and distances are ranked with electron spin resonance (ESR). We have found that there is a significant amount of 3(10)-helix in 16-residue model peptides containing only L-amino acids. This review covers several facets of the methodology including spin labeling strategy, interpretation of ESR spectra and the influence of molecular dynamics on the spectral line shapes. Also covered are recent findings of a length-dependent 3(10)-helix-->alpha-helix transition and the role of Arg+ in the stabilization of specific helix structures.
在过去几年中，我们使用自旋标记作为探索螺旋肽结构的一种方法。将两个氮氧化物标记引入肽序列中，并通过电子自旋共振（ESR）对距离进行排序。我们发现，在仅含L-氨基酸的16残基模型肽中存在大量3(10)-螺旋。本综述涵盖了该方法的几个方面，包括自旋标记策略、ESR光谱的解读以及分子动力学对谱线形状的影响。还涵盖了关于长度依赖性3(10)-螺旋向α-螺旋转变的最新发现以及Arg+在特定螺旋结构稳定中的作用。
