Eva Meirovitch

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The dynamics of adenylate kinase of Escherichia coli (AKeco) and its complex with the inhibitor AP(5)A, are characterized by correlating the theoretical results obtained with the Gaussian Network Model (GNM) and the anisotropic network model (ANM) with the order parameters and correlation times obtained with Slowly Relaxing Local Structure (SRLS) analysis(More)
The focus of structural biology is on studies of the highly populated, ground states of biological molecules; states that are only sparsely and transiently populated are more difficult to probe because they are invisible to most structural methods. Yet, such states can play critical roles in biochemical processes such as ligand binding, enzyme catalysis,(More)
Enhanced internal mobility in proteins is typically functional. Domain motion in enzymes, necessarily related to catalysis, is a prototype in this context. Experimental (15)N spin relaxation data from E. coli adenylate kinase report qualitatively on nanosecond motion experienced by the domains AMPbd and LID. Previous quantitative analysis based on the(More)
NMR spin relaxation of (2)H nuclei in (13)CH(2)D groups is a powerful method for studying side-chain motion in proteins. The analysis is typically carried out with the original model-free (MF) approach adapted to methyl dynamics. The latter is described in terms of axial local motions around, and of, the methyl averaging axis, mutually decoupled and(More)
Restricted motions in proteins (e.g., N-H bond dynamics) are studied effectively with NMR. By analogy with restricted motions in liquid crystals (LC), the local ordering has in the past been primarily represented by potentials comprising the L = 2, |K| = 0, 2 spherical harmonics. However, probes dissolved in LCs experience nonpolar ordering, often referred(More)
Deuterium line shape analysis from mobile C-D and C-CD3 groups has emerged as a particularly useful tool for studying dynamics in the solid state. The theoretical models devised so far consist typically of sets of independent dynamic modes. Each such mode is simple and usually case-specific. In this scenario, model improvement entails adding yet another(More)
We applied over a decade ago the two-body coupled-rotator slowly relaxing local structure (SRLS) approach to NMR relaxation in proteins. One rotator is the globally moving protein and the other rotator is the locally moving probe (spin-bearing moiety, typically the (15)N-(1)H bond). So far we applied SRLS to (15)N-H relaxation from seven different proteins(More)
We developed in recent years the two-body (protein and probe) coupled-rotator slowly relaxing local structure (SRLS) approach for elucidating protein dynamics from NMR spin relaxation. So far we used as descriptors the set of physical parameters that enter the SRLS model. They include the global (protein-related) diffusion tensor, D1, the local(More)
15N–H relaxation parameters from ribonuclease HI (RNase H), acquired in previous work at magnetic fields of 14.1 and 18.8 T, and at 300 K, are analyzed with the mode-coupling slowly relaxing local structure (SRLS) approach. In accordance with standard theoretical treatments of restricted motions, SRLS approaches N-H bond dynamics from a tensorial(More)