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1.

NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
by Sekhar, Ashok

Proceedings of the National Academy of Sciences of the United States of America, August 6, 2013, Vol.110(32), pp.12867-12874

2.

Transiently populated intermediate functions as a branching point of the FF domain folding pathway.
by Korzhnev, Dmitry M

Proceedings of the National Academy of Sciences of the United States of America, October 30, 2012, Vol.109(44), pp.17777-17782

3.

Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain.
by Murphy, James M

Proceedings of the National Academy of Sciences of the United States of America, September 4, 2007, Vol.104(36), pp.14336-14341

4.

Proteasome allostery as a population shift between interchanging conformers.
by Ruschak, Amy M

Proceedings of the National Academy of Sciences of the United States of America, December 11, 2012, Vol.109(50), pp.E3454-E3462

5.

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy.
by Vallurupalli, Pramodh

Proceedings of the National Academy of Sciences of the United States of America, August 19, 2008, Vol.105(33), pp.11766-11771

7.

Solution NMR-derived global fold of a monomeric 82-kDa enzyme.
by Tugarinov, Vitali

Proceedings of the National Academy of Sciences of the United States of America, 2005, Vol.102(3), pp.622-7

8.

Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release.
by Sprangers, Remco

Proceedings of the National Academy of Sciences of the United States of America, November 15, 2005, Vol.102(46), pp.16678-16683

9.

Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.
by Donaldson, Logan W

Proceedings of the National Academy of Sciences of the United States of America, October 29, 2002, Vol.99(22), pp.14053-14058

10.

Site-specific contributions to the pH dependence of protein stability.
by Tollinger, Martin

Proceedings of the National Academy of Sciences of the United States of America, April 15, 2003, Vol.100(8), pp.4545-4550

11.

Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site.
by Mazhab-Jafari, Mohammad T

Proceedings of the National Academy of Sciences of the United States of America, May 26, 2015, Vol.112(21), pp.6625-6630

12.

Tracing an allosteric pathway regulating the activity of the HslV protease.
by Shi, Lichi

Proceedings of the National Academy of Sciences of the United States of America, February 11, 2014, Vol.111(6), pp.2140-2145

13.

Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
by Huang, Rui

Proceedings of the National Academy of Sciences of the United States of America, July 19, 2016, Vol.113(29), pp.E4190-E4199

14.

Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.
by Sekhar, Ashok

Proceedings of the National Academy of Sciences of the United States of America, November 20, 2012, Vol.109(47), pp.19268-19273

15.

Measurement of bond vector orientations in invisible excited states of proteins.
by Vallurupalli, Pramodh

Proceedings of the National Academy of Sciences of the United States of America, November 20, 2007, Vol.104(47), pp.18473-18477

16.

ClpB N-terminal domain plays a regulatory role in protein disaggregation.
by Rosenzweig, Rina

Proceedings of the National Academy of Sciences of the United States of America, December 15, 2015, Vol.112(50), pp.E6872-E6881

17.

Measuring hydrogen exchange rates in invisible protein excited states.
by Long, Dong

Proceedings of the National Academy of Sciences of the United States of America, June 17, 2014, Vol.111(24), pp.8820-8825

18.

Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR.
by Kotler, Samuel A

Proceedings of the National Academy of Sciences of the United States of America, February 26, 2019, Vol.116(9), pp.3562-3571

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