The quiet renaissance of protein nuclear magnetic resonance.
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.
Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, United States.
Paul J
PJ
Barrett
Jiang
J
Chen
Min-Kyu
MK
Cho
Ji-Hun
JH
Kim
Zhenwei
Z
Lu
Sijo
S
Mathew
Dungeng
D
Peng
Yuanli
Y
Song
Wade D
WD
Van Horn
Tiandi
T
Zhuang
Frank D
FD
Sönnichsen
Charles R
CR
Sanders
D000818:Animals; D055808:Drug Discovery; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000266:history / Q000379:methods*; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000266:history / Q000379:methods; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D011506:Proteins