SRLS analysis of 15N spin relaxation from E. coli ribonuclease HI: The tensorial perspective

Eva Meirovitch, Yury E. Shapiro, Mirco Zerbetto, Antonino Polimeno

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations


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 perspective. As shown previously, a physically adequate description of this phenomenon has to account for the asymmetry of the local spatial restrictions. So far, we used rhombic local ordering tensors; this is straightforward but computationally demanding. Here, we propose substantiating the asymmetry of the local spatial restrictions in terms of tilted axial local ordering (S) and local diffusion (D2) tensors. Although less straightforward, this description provides physically sound structural and dynamic information and is efficient computationally. We find that the local order parameter, S02, is on average 0.89 (0.84, and may be as small as 0.6) for the secondary structure elements (loops). The main local ordering axis deviates from the Ci-1 α-Ciα axis by less than 6°. At 300 K, D2,⊥ is virtually the same as the global diffusion rate, D 1 = 1.8 × 107 s-1. The correlation time 1/6D2,∥ ranges from 3-125 (208-344) ps for the secondary structure elements (loops) and is on average 125 ps for the C-terminal segment. The main local diffusion axis deviates from the N-H bond by less than 2° (10°) for the secondary structure elements (loops). An effective data-fitting protocol, which leads in most cases to unambiguous results with limited uncertainty, has been devised. A physically sound and computationally effective methodology for analyzing 15N relaxation in proteins, that provides a new picture of N-H bond structural dynamics in proteins, has been set forth.

Original languageEnglish
Pages (from-to)886-894
Number of pages9
JournalJournal of Physical Chemistry B
Issue number2
StatePublished - 19 Jan 2012


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