CHEMICAL-SHIFT RANGES IN PROTEINS

被引：80

作者：

AUGSPURGER, J ^{[1
]}

PEARSON, JG ^{[1
]}

OLDFIELD, E ^{[1
]}

DYKSTRA, CE ^{[1
]}

PARK, KD ^{[1
]}

SCHWARTZ, D ^{[1
]}

机构：

[1] UNIV ILLINOIS,DEPT CHEM,URBANA,IL 61801

来源：

JOURNAL OF MAGNETIC RESONANCE | 1992年 / 100卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0022-2364(92)90267-B

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The results of ab initio derivative Hartree-Fock calculations of the dipole and quadrupole shielding polarizabilities and hyperpolarizabilities of a number of small molecules are reported, together with estimates of the electric fields and field gradients present in proteins. It is argued that weak electrical interactions, mediated via these shielding polarizabilities, make major contributions to the chemical-shift nonequivalencies observed in proteins due to folding into their native conformations. The electric-field-induced shifts may be very large (≈5 ppm for 13C, ≈10 ppm for 17O and 17F), due to the low dielectric constants found in proteins, and in some cases they may dominate the experimentally observed spectral shifts. © 1992.

引用

页码：342 / 357

页数：16

共 58 条

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