Pitfalls in measurements of R₁ relaxation rates of protein backbone ¹⁵N nuclei.

ABSTRACT: The dynamics of the backbone and side-chains of protein are routinely studied by interpreting experimentally determined ¹⁵N spin relaxation rates. R₁(¹⁵N), the longitudinal relaxation rate, reports on fast motions and encodes, together with the transverse relaxation R₂, structural information about the shape of the molecule and the orientation of the amide bond vectors in the internal diffusion frame. Determining error-free ¹⁵N longitudinal relaxation rates remains a challenge for small, disordered, and medium-sized proteins. Here, we show that mono-exponential fitting is sufficient, with no statistical preference for bi-exponential fitting up to 800 MHz. A detailed comparison of the TROSY and HSQC techniques at medium and high fields

SUBMITTER: Kharchenko V 

PROVIDER: S-EPMC11832611 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature