Abstract
Spin-lattice relaxation times ( T 1) have been measured at 100 MHz with the pulse Fourier transform NMR method for nonexchangeable protons of yeast tRNA Phe in the neutral D 2O solution as a function of temperature. The proton relaxation times were simulated by the use of X-ray-structure coordinates and the rotational correlation times deduced from 31P magnetic relaxation measurements. For the ribose protons (2′-5′) the simulated relaxation times closely agree with the experimental ones, indicating that the molecular motion as viewed through the ribose protons is the same as that observed through phosphorus, and therefore that all sections of ribose-phosphate part are characterized by common correlation times. For the ribose 1′ and the base protons, experimentally obtained T 1 values show much less temperature dependence than those calculated, suggesting that there is a wider distribution in the rotational correlation times in the base part than in the ribose-phosphate part.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
