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蛋白质中抗磁各向异性的结构起源

Structural origins of diamagnetic anisotropy in proteins.

作者信息

Worcester D L

出版信息

Proc Natl Acad Sci U S A. 1978 Nov;75(11):5475-7. doi: 10.1073/pnas.75.11.5475.

DOI:10.1073/pnas.75.11.5475
PMID:281695
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC392987/
Abstract

Magnetic anisotropy in proteins and polypeptides can be attributed to the diamagnetic anisotropy of the planar peptide bonds. The alpha helix in particular has large anisotropy due to the axial alignment of the peptide bonds. The regular arrangements of the peptide bonds in beta pleated sheet and collagen structures also produce substantial anisotropy, but less than for alpha helix. The anisotropy permits orientation of small structures of these types in magnetic fields of several kilogauss.

摘要

蛋白质和多肽中的磁各向异性可归因于平面肽键的抗磁各向异性。特别是α螺旋，由于肽键的轴向排列而具有较大的各向异性。β折叠片和胶原蛋白结构中肽键的规则排列也会产生相当大的各向异性，但比α螺旋要小。这种各向异性使得这些类型的小结构能够在几千高斯的磁场中取向。