Nuclear Magnetic Resonance in the Era of Structural Genomics
Document Type
Article
Subject Area(s)
NMR, Nuclear Magnetic Resonance, structural genomics, X-ray, X-ray diffraction
Abstract
Current interests in structural genomics, and the associated need for high through-put structure determination methods, offer an opportunity to examine new nuclear magnetic resonance (NMR) methodology and the impact this methodology can have on structure determination of proteins. The time required for structure determination by traditional NMR methods is currently long, but improved hardware, automation of analysis, and new sources of data such as residual dipolar couplings promise to change this. Greatly improved efficiency, coupled with an ability to characterize proteins that may not produce crystals suitable for investigation by X-ray diffraction, suggests that NMR will play an important role in structural genomics programs.
Publication Info
Published in Biochemistry, Volume 40, Issue 30, Summer 2001, pages 8677-8685.
©Biochemistry 2001, American Chemistry Society
Prestegard, J., Valafar, H., Glushka, J., & Tian, F. (2001). Nuclear Magnetic Resonance in the Era of Structural Genomics†. Biochemistry, 40(30), 8677-8685. doi: 10.1021/bi0102095
Rights
©Biochemistry 2001, American Chemistry Society
Prestegard, J., Valafar, H., Glushka, J., & Tian, F. (2001). Nuclear Magnetic Resonance in the Era of Structural Genomics†. Biochemistry, 40(30), 8677-8685. doi: 10.1021/bi0102095