Work

The Quiet Renaissance of Protein Nuclear Magnetic Resonance

Year: 2013

Type: article

Abstract: From roughly 1985 through the start of the new millennium, the cutting edge of solution protein nuclear magnetic resonance (NMR) spectroscopy was to a significant extent driven by the aspiration to determine structures. Here we survey recent advances in protein NMR that herald a renaissance in which a number of its most important applications reflect the broad problem-solving capability displayed by this method during its classical era during the 1970s and early 1980s.

Source: Biochemistry

DOI: 10.1021/bi4000436

Authors: Paul J. Barrett, Jiang Chen, Min-Kyu Cho, Ji-Hun Kim, Zhenwei Lu, Sijo Mathew, Dungeng Peng, Yuanli Song, Wade D. Van Horn, Tiandi Zhuang, Frank D. Sönnichsen, Charles R. Sanders

Institutions: Vanderbilt University, Arizona State University, University of Virginia, Christian-Albrechts-Universität zu Kiel

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: Amgen, National Institutes of Health, U.S. Public Health Service, National Institute on Deafness and Other Communication Disorders, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Neurological Disorders and Stroke

Awards: G1104128699, G18496906, Protein Structure and Dynamics from EPR Spectroscopy and MD Simulations, Structure Function Analysis of Integrins alpha1beta1 and alpha2beta2, G3485139178, G4786617886, G5743428282, G6742580802, G7183911145

OpenAlex ID: W2097587930

FWCI: 3.144

Cites: 181

Cited by: 50

Related to: 10