A Review of REDCRAFT: Simultaneous Investigation of Structure and Dynamics of Proteins from RDC Restraints

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Article

Abstract

Residual dipolar couplings (RDCs) have emerged as a viable source of NMR data for the study of protein structure and dynamics. Although very informative and accurate, their use has been limited because of challenges associated with comprehensive analyses of RDC data. The REDCRAFT software package has been designed to use RDCs exclusively for the simultaneous study of protein structure and dynamics. This has enabled the direct study of protein backbones and facilitated the fragmented study of proteins for instances where only partial data may be available. REDCRAFT's effective search engine has also resulted in a reduction in the number of RDC data required per residue to near theoretical limits. Here, we demonstrate the ability of REDCRAFT in structure determination of proteins using only backbone {N–H, Cα–Hα} RDCs from two alignment media, or {C–N, N–H, C–H} from one alignment medium and {N–H} from the second alignment medium. In addition, we present the success of REDCRAFT in identification of internal dynamics and its proper treatment in application to simulated data.

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© Annual Reports on NMR Spectroscopy 2012, Elsevier

Valafar, H., Simin, M., & Irausquin, S. (2012). A Review of REDCRAFT: Simultaneous Investigation of Structure and Dynamics of Proteins from RDC Restraints. Annual Reports On NMR Spectroscopy, 76, 23-66. doi: 10.1016/b978-0-12-397019-0.00002-9

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