Use of Measured Residual Dipolar Couplings to Calculate Residual Dipolar Couplings for a Protein Structure: A Case Study Using Hen Egg-White Lysozyme.

ABSTRACT: Five sets of RDC values for the backbone of [¹³C,¹⁵N]-labeled Hen Egg-White Lysozyme (HEWL, 320 RDCs), obtained from NMR experiments of the protein in an ether bicelle solution at a temperature of 308 K and pH 3.8, were used to calculate RDC values by application of two methods, the alignment-tensor (AT) method and the method of magnetic-field rotational sampling (HRS), applied to five X-ray structures of HEWL, to investigate the relevance of measured RDC values for the structure determination or refinement of proteins. In contrast to other quantities Q observable by NMR, such as NOE intensities or ³J-couplings, for which a relation Q(r) between the quantity Q and a single structure r of a protein can be used to cal

SUBMITTER: Pechlaner M 

PROVIDER: S-EPMC12529780 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature