Distance between phosphine-sulfide sidechains of a disubstituted peptide by DRAMA P-31 NMR

被引：4

作者：

Klug, CA ^{[1
]}

Studelska, DR ^{[1
]}

Chen, GH ^{[1
]}

Gilbertson, SR ^{[1
]}

Schaefer, J ^{[1
]}

机构：

[1] WASHINGTON UNIV,DEPT CHEM,ST LOUIS,MO 63130

来源：

SOLID STATE NUCLEAR MAGNETIC RESONANCE | 1996年 / 7卷 / 03期

关键词：

lyoprotectants; phosphine-sulfide peptides; solid-sate NMR;

D O I：

10.1016/S0926-2040(96)01268-4

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：

Dipolar restoration at the magic angle (DRAMA) has been used to measure the P-31-P-31 internuclear distance between phosphine-sulfide substituted sidechains on the fourth and eighth residues of a 12-residue helical peptide. The 7.4 Angstrom distance is the same for the peptide lyophilized in bulk or isolated in a cryo- and lyoprotected matrix of poly(ethylene glycol) and sucrose. However, the P-31 linewidth for the undiluted peptide is an order of magnitude greater than for the matrix-isolated peptide indicating charge and hydration heterogeneity in the bulk state.

引用

页码：173 / 176

页数：4

共 15 条

[1]

CHEN G, THESIS WASHINGTON U

[2] SOLID-STATE NMR DETERMINATION OF INTRAMOLECULAR AND INTERMOLECULAR P-31-C-13 DISTANCES FOR SHIKIMATE 3-PHOSPHATE AND [1-C-13]GLYPHOSATE BOUND TO ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE [J].