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1.

Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.
by Hoeltzli, S D

Proceedings of the National Academy of Sciences of the United States of America, September 26, 1995, Vol.92(20), pp.9318-9322

2.

Contacting the protein folding funnel with NMR.
by Onuchic, J N

Proceedings of the National Academy of Sciences of the United States of America, July 8, 1997, Vol.94(14), pp.7129-7131

3.

Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.
by Kovacs, F

Proceedings of the National Academy of Sciences of the United States of America, July 6, 1999, Vol.96(14), pp.7910-7915

4.

Extending the size limit of protein nuclear magnetic resonance.
by Yu, H

Proceedings of the National Academy of Sciences of the United States of America, January 19, 1999, Vol.96(2), pp.332-334

6.

Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.
by Arcus, V L

Proceedings of the National Academy of Sciences of the United States of America, September 27, 1994, Vol.91(20), pp.9412-9416

7.

De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates.
by Fezoui, Y

Proceedings of the National Academy of Sciences of the United States of America, April 26, 1994, Vol.91(9), pp.3675-3679

8.

Solution structure and dynamics of a de novo designed three-helix bundle protein.
by Walsh, S T

Proceedings of the National Academy of Sciences of the United States of America, May 11, 1999, Vol.96(10), pp.5486-5491

9.

Detection of residue contacts in a protein folding intermediate
by Balbach, Jochen

Proceedings of the National Academy of Sciences of the United States, July 8, 1997, Vol.94(14), p.7182(4)

10.

Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies.
by Xu, R

Proceedings of the National Academy of Sciences of the United States of America, January 19, 1999, Vol.96(2), pp.388-393

11.

The folding pathway of a protein at high resolution from microseconds to seconds.
by Nölting, B

Proceedings of the National Academy of Sciences of the United States of America, February 4, 1997, Vol.94(3), pp.826-830

12.

Role of the J-domain in the cooperation of Hsp40 with Hsp70
by Greene, Michael K.

Proceedings of the National Academy of Sciences of the United States, May 26, 1998, Vol.95(11), p.6108(6)

13.

The histone fold: evolutionary questions
by Ramakrishnan, V.

Proceedings of the National Academy of Sciences of the United States, Dec 5, 1995, Vol.92(25), p.11328(3)

14.

Initiation sites of protein folding by NMR analysis.
by Freund, S M

Proceedings of the National Academy of Sciences of the United States of America, October 1, 1996, Vol.93(20), pp.10600-10603

16.

Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.
by Jacobs, M D

Proceedings of the National Academy of Sciences of the United States of America, January 18, 1994, Vol.91(2), pp.449-453

17.

Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy.
by Peng, X

Proceedings of the National Academy of Sciences of the United States of America, March 1, 1993, Vol.90(5), pp.1776-1780

18.

Synergy between simulation and experiment in describing the energy landscape of protein folding.
by Ladurner, A G

Proceedings of the National Academy of Sciences of the United States of America, July 21, 1998, Vol.95(15), pp.8473-8478

19.

Conformational influences of glycosylation of a peptide: a possible model for the effect of glycosylation on the rate of protein folding.
by Live, D H

Proceedings of the National Academy of Sciences of the United States of America, November 12, 1996, Vol.93(23), pp.12759-12761

20.

The early stage of folding of villin headpiece subdomain observed in a 200-nanosecond fully solvated molecular dynamics simulation.
by Duan, Y

Proceedings of the National Academy of Sciences of the United States of America, August 18, 1998, Vol.95(17), pp.9897-9902

123

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