Automated protein structure calculation from NMR data

• Published in: Journal of biomolecular NMR Vol. 43; no. 3; pp. 131 - 143
• Main Authors: Williamson, Mike P, Craven, C. Jeremy
• Format: Journal Article
• Language: English
• Published: Dordrecht Dordrecht : Springer Netherlands 01-03-2009; Springer Netherlands; Springer Nature B.V
• Subjects: Automation; Biochemistry; Biological and Medical Physics; Biophysics; Genomics; NMR; Nuclear magnetic resonance; Nuclear Magnetic Resonance, Biomolecular; Perspective; Physics; Physics and Astronomy; Protein Conformation; Proteins - chemistry; Sample preparation; Signal Processing, Computer-Assisted; Software; Spectroscopy/Spectrometry; Spectrum analysis; Programs; NMR structure calculation of proteins; Automation; Structural genomics; Expert
• ISSN: 0925-2738; 1573-5001
• DOI: 10.1007/s10858-008-9295-6

Current software is almost at the stage to permit completely automatic structure determination of small proteins of <15 kDa, from NMR spectra to structure validation with minimal user interaction. This goal is welcome, as it makes structure calculation more objective and therefore more easily validated, without any loss in the quality of the structures generated. Moreover, it releases expert spectroscopists to carry out research that cannot be automated. It should not take much further effort to extend automation to ca 20 kDa. However, there are technological barriers to further automation, of which the biggest are identified as: routines for peak picking; adoption and sharing of a common framework for structure calculation, including the assembly of an automated and trusted package for structure validation; and sample preparation, particularly for larger proteins. These barriers should be the main target for development of methodology for protein structure determination, particularly by structural genomics consortia.