13C nuclear magnetic resonance relaxation-derived psi, phi bond rotational energy barriers and rotational restrictions for glycine 13C alpha-methylenes in a GXX-repeat hexadecapeptide.
13C nuclear magnetic resonance relaxation-derived psi, phi bond rotational energy barriers and rotational restrictions for glycine 13C alpha-methylenes in a GXX-repeat hexadecapeptide.
复制标题
13C 核磁共振弛豫衍生的 psi、phi 键旋转能垒和 GXX 重复十六肽中甘氨酸 13C α-亚甲基的旋转限制。
DOI：
10.1021/bi00091a007
复制
发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Mayo,KH
中科院分区：
文献类型：
--
作者：
Daragan,VA;Kloczewiak,MA;Mayo,KH
Revised Manuscript Received July 28, 1993z abstract: Spin-lattice relaxation of 13C multiplet spectra and {}-13C nuclear Overhauser enhancement (NOE) coefficients of selectively 13C-enriched glycines in a collagen GXX-repeat motif hexadecapeptide, GiVKG4DKG7NPG10WPG 13APY, has been investigated. Data have been collected at two 13C Larmor frequencies (90 and 150 MHz) over the temperature range from 5 to 70 C. Relaxation data indicate that the most restricted internal rotations are at G7 and G10. Mobility of other glycine residues can be arranged in the order G4, Gl3, and Gl. Gl glycine shows the least change in motional anisotropy with temperature. Several motional models have been used to explain the experimental data. While any one model is not completely satisfactory in describing all experimental parameters, only the model of restricted internal diffusion yields theobserved positive sign for the cross-correlated spectral densities. Energetic and angular limits of, bond rotational motions derived from relaxation data and the restricteddiffusion model are in good agreement with those calculated as Ramachandran potentional energy profiles. Gl rotational energy barriers for overall tumbling and internal rotation are approximately equal, suggesting strong interaction between the N-terminus and water. Internal rotational parameters for GV and GG dipeptides confirm this view. Nonterminal glycine internal motions are apparently less dependent on water-peptide interactions.
