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1.

A hypothesis to reconcile the physical and chemical unfolding of proteins.
by de Oliveira, Guilherme A P

Proceedings of the National Academy of Sciences of the United States of America, May 26, 2015, Vol.112(21), pp.E2775-E2784

2.

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

3.

Physics-based method to validate and repair flaws in protein structures.
by Martin, Osvaldo A

Proceedings of the National Academy of Sciences of the United States of America, October 15, 2013, Vol.110(42), pp.16826-16831

4.

Cavities determine the pressure unfolding of proteins.
by Roche, Julien

Proceedings of the National Academy of Sciences of the United States of America, May 1, 2012, Vol.109(18), pp.6945-6950

5.

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

6.

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

7.

Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction.
by Scian, Michele

Proceedings of the National Academy of Sciences of the United States of America, July 31, 2012, Vol.109(31), pp.12521-12525

8.

Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.
by Zhang, Shuai

Proceedings of the National Academy of Sciences of the United States of America, February 19, 2013, Vol.110(8), pp.2798-2803

9.

Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
by Aznauryan, Mikayel

Proceedings of the National Academy of Sciences of the United States of America, September 13, 2016, Vol.113(37), pp.E5389-E5398

10.

Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.
by Bista, Michal

Proceedings of the National Academy of Sciences of the United States of America, September 25, 2012, Vol.109(39), pp.15752-15756

11.

Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.
by Liang, Binyong

Proceedings of the National Academy of Sciences of the United States of America, November 26, 2013, Vol.110(48), pp.19384-19389

12.

Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.
by Libich, David S

Proceedings of the National Academy of Sciences of the United States of America, July 21, 2015, Vol.112(29), pp.8817-8823

13.

Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
by Charlier, Cyril

Proceedings of the National Academy of Sciences of the United States of America, May 1, 2018, Vol.115(18), pp.E4169-E4178

14.

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.
by Kadavath, Harindranath

Proceedings of the National Academy of Sciences of the United States of America, June 16, 2015, Vol.112(24), pp.7501-7506

15.

A high-affinity, dimeric inhibitor of PSD-95 bivalently interacts with PDZ1-2 and protects against ischemic brain damage.
by Bach, Anders

Proceedings of the National Academy of Sciences of the United States of America, February 28, 2012, Vol.109(9), pp.3317-3322

16.

The acquisition of multidimensional NMR spectra within a single scan.
by Frydman, Lucio

Proceedings of the National Academy of Sciences of the United States of America, December 10, 2002, Vol.99(25), pp.15858-15862

17.

Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.
by Robertson, Amy L

Proceedings of the National Academy of Sciences of the United States of America, June 8, 2010, Vol.107(23), pp.10424-10429

18.

ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.
by Evans, Matthew R

Proceedings of the National Academy of Sciences of the United States of America, February 24, 2009, Vol.106(8), pp.2617-2622

19.

The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein.
by Teilum, Kaare

Proceedings of the National Academy of Sciences of the United States of America, May 2, 2006, Vol.103(18), pp.6877-6882

20.

Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution.
by Kazmirski, S L

Proceedings of the National Academy of Sciences of the United States of America, April 10, 2001, Vol.98(8), pp.4349-4354

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