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蛋白质溶液和生物系统的双折射。I.

Birefringence of protein solutions and biological systems. I.

作者信息

TAYLOR E W, CRAMER W

出版信息

Biophys J. 1963 Mar;3(2):127-41. doi: 10.1016/s0006-3495(63)86809-5.

DOI:10.1016/s0006-3495(63)86809-5
PMID:13993579
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1366431/
Abstract

The quantitative interpretation of birefringence of biological structures such as muscle requires a knowledge of intrinsic birefringence of the components. The intrinsic birefringence of fibrous structures as determined by variation of solvent index is positive while the intrinsic birefringence of proteins in solution is negative as calculated by the Peterlin-Stuart theory. As a first step in clarifying this discrepancy the basis of the Peterlin-Stuart theory has been re-examined. The theory has been recalculated from the standpoint of light scattering and extended to particles whose length is not small compared to the wavelength. The birefringence of a system of particles possessing a shell with index different from the bulk solvent has been obtained in order to interpret measurements in mixed solvents.

摘要

对诸如肌肉等生物结构双折射的定量解释需要了解其组成成分的固有双折射。由溶剂折射率变化所确定的纤维结构的固有双折射为正,而根据彼得林 - 斯图尔特理论计算,溶液中蛋白质的固有双折射为负。作为澄清这一差异的第一步,对彼得林 - 斯图尔特理论的基础进行了重新审视。该理论已从光散射的角度重新计算,并扩展到长度与波长相比不小的粒子。为了解释在混合溶剂中的测量结果,已得出具有与主体溶剂折射率不同的壳层的粒子系统的双折射。

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本文引用的文献

1
Structure and enzymatic break-down of proteins.蛋白质的结构与酶促分解
Cold Spring Harb Symp Quant Biol. 1950;14:117-26. doi: 10.1101/sqb.1950.014.01.016.