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1.

Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
by Granata, Daniele

Proceedings of the National Academy of Sciences of the United States of America, April 23, 2013, Vol.110(17), pp.6817-6822

2.

Defining a length scale for millisecond-timescale protein conformational exchange
by Sekhar, Ashok

Proceedings of the National Academy of Sciences of the United States of America, Jul 9, 2013, Vol.110(28), p.11391

3.

Toward an atomistic description of the urea-denatured state of proteins.
by Candotti, Michela

Proceedings of the National Academy of Sciences of the United States of America, April 9, 2013, Vol.110(15), pp.5933-5938

5.

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

6.

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

7.

Control over overall shape and size in de novo designed proteins.
by Lin, Yu-Ru

Proceedings of the National Academy of Sciences of the United States of America, October 6, 2015, Vol.112(40), pp.E5478-E5485

8.

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

9.

Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication
by Leigh, Kendra

Proceedings of the National Academy of Sciences of the United States of America, Jul 21, 2015, Vol.112(29), p.9010

10.

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

11.

Preventing fibril formation of a protein by selective mutation
by Maisuradze, Gia

Proceedings of the National Academy of Sciences, USA, November 2015, Vol.112(44), p.13549

12.

Thermodynamics of protein destabilization in live cells.
by Danielsson, Jens

Proceedings of the National Academy of Sciences of the United States of America, October 6, 2015, Vol.112(40), pp.12402-12407

13.

Measurement of histidine pKa values and tautomer populations in invisible protein states.
by Hansen, Alexandar L

Proceedings of the National Academy of Sciences of the United States of America, April 29, 2014, Vol.111(17), pp.E1705-E1712

14.

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

15.

Role of cavities and hydration in the pressure unfolding of T^sub 4^ lysozyme
by Nucci, Nathaniel

Proceedings of the National Academy of Sciences of the United States of America, Sep 23, 2014, Vol.111(38), p.13846

16.

N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.
by Karagöz, G Elif

Proceedings of the National Academy of Sciences of the United States of America, January 11, 2011, Vol.108(2), pp.580-585

17.

Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy.
by Eichmann, Cédric

Proceedings of the National Academy of Sciences of the United States of America, May 18, 2010, Vol.107(20), pp.9111-9116

18.

Structure of an intermediate conformer of the spindle checkpoint protein Mad2.
by Hara, Mayuko

Proceedings of the National Academy of Sciences of the United States of America, September 8, 2015, Vol.112(36), pp.11252-11257

19.

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

20.

High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.
by Vajpai, Navratna

Proceedings of the National Academy of Sciences of the United States of America, January 29, 2013, Vol.110(5), pp.E368-E376

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