The in situ structure of ribosomal proteins from polarized neutron scattering

被引：17

作者：

Willumeit, R ^{[1
]}

Burkhardt, N ^{[1
]}

Diedrich, G ^{[1
]}

Zhao, J ^{[1
]}

Nierhaus, KH ^{[1
]}

Stuhrmann, HB ^{[1
]}

机构：

[1] MAX PLANCK INST MOL GENET,D-14195 BERLIN,GERMANY

来源：

JOURNAL OF MOLECULAR STRUCTURE | 1996年 / 383卷 / 1-3期

关键词：

neutron scattering; isotopic substitution; ribosomal proteins;

D O I：

10.1016/S0022-2860(96)09287-3

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Methods of isotopic substitution are widely used in neutron scattering for the determination of the in situ structure of macromolecular components. The contrast created by substitution of the hydrogen isotope H-1 (proton) by H-2 (deuteron) is the most prominent example in contrast variation. A further increase of the contrast is achieved if a polarized neutron beam is scattered by polarized nuclear spins in the sample. This so called spin-contrast-variation method is used to determine the position of the protein L1 in the 50S subunit of the E. coli ribosome and proteins S6 and S10 in the 70S ribosome.

引用

页码：201 / 211

页数：11

共 46 条

[1]

ABRAGAM A, 1982, NUCLEAR MAGNETISM OR

[2] ASPECTS IN STRUCTURAL STUDIES ON RIBOSOMES [J].