| Year |
Citation |
Score |
| 2012 |
Chung JK, Thielges MC, Lynch SR, Fayer MD. Fast dynamics of HP35 for folded and urea-unfolded conditions. The Journal of Physical Chemistry. B. 116: 11024-31. PMID 22909017 DOI: 10.1021/Jp304058X |
0.766 |
|
| 2012 |
Chung JK, Thielges MC, Fayer MD. Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes. Journal of the American Chemical Society. 134: 12118-24. PMID 22764745 DOI: 10.1021/Ja303017D |
0.758 |
|
| 2012 |
Thielges MC, Chung JK, Fayer MD. Dynamics at Specific Sites in Proteins Studied by 2D IR Vibrational Echo Spectroscopy Biophysical Journal. 102: 224a-225a. DOI: 10.1016/J.Bpj.2011.11.1233 |
0.778 |
|
| 2011 |
Thielges MC, Axup JY, Wong D, Lee HS, Chung JK, Schultz PG, Fayer MD. Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand. The Journal of Physical Chemistry. B. 115: 11294-304. PMID 21823631 DOI: 10.1021/Jp206986V |
0.77 |
|
| 2011 |
Thielges MC, Chung JK, Axup JY, Fayer MD. Influence of histidine tag attachment on picosecond protein dynamics. Biochemistry. 50: 5799-805. PMID 21619030 DOI: 10.1021/Bi2003923 |
0.75 |
|
| 2011 |
Chung JK, Thielges MC, Bowman SE, Bren KL, Fayer MD. Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments. Journal of the American Chemical Society. 133: 6681-91. PMID 21469666 DOI: 10.1021/Ja111009S |
0.747 |
|
| 2011 |
Thielges MC, Chung JK, Fayer MD. Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy. Journal of the American Chemical Society. 133: 3995-4004. PMID 21348488 DOI: 10.1021/Ja109168H |
0.742 |
|
| 2011 |
Chung JK, Thielges MC, Fayer MD. Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 108: 3578-83. PMID 21321226 DOI: 10.1073/Pnas.1100587108 |
0.703 |
|
| 2010 |
Chung JK, Thielges MC, Bowman S, Bren K, Fayer MD. Ultrafast Dynamics of Thermal Denaturation of Cytochrome-C with Two Dimensional Infrared Spectroscopy Biophysical Journal. 98: 441a. DOI: 10.1016/J.Bpj.2009.12.2398 |
0.758 |
|
| 2010 |
Thielges MC, Chung JK, Fayer MD. The Contribution of Fast Protein Dynamics to Cytochrome P450 Molecular Recognition Characterized by Two-Dimensional Infrared Spectroscopy Biophysical Journal. 98: 234a. DOI: 10.1016/J.Bpj.2009.12.1270 |
0.745 |
|
| 2008 |
Kwak K, Rosenfeld DE, Chung JK, Fayer MD. Solute-solvent complex switching dynamics of chloroform between acetone and dimethylsulfoxide-two-dimensional IR chemical exchange spectroscopy. The Journal of Physical Chemistry. B. 112: 13906-15. PMID 18855462 DOI: 10.1021/Jp806035W |
0.676 |
|
| 2008 |
Kim S, Chung JK, Kwak K, Bowman SE, Bren KL, Bagchi B, Fayer MD. Native and unfolded cytochrome c--comparison of dynamics using 2D-IR vibrational echo spectroscopy. The Journal of Physical Chemistry. B. 112: 10054-63. PMID 18646797 DOI: 10.1021/Jp802246H |
0.602 |
|
| 2008 |
Ishikawa H, Kwak K, Chung JK, Kim S, Fayer MD. Direct observation of fast protein conformational switching. Proceedings of the National Academy of Sciences of the United States of America. 105: 8619-24. PMID 18562286 DOI: 10.1073/Pnas.0803764105 |
0.631 |
|
| 2008 |
Ishikawa H, Kwak K, Chung JK, Kim S, Fayer MD. 1P-102 Fast protein conformational switching observed with 2D-IR vibrational echo(Invited Talk for Early Research in Biophysics Award,Early Research in Biophysics Award)(The 46th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 48: S37. DOI: 10.2142/Biophys.48.S37_1 |
0.513 |
|
| 2007 |
Ishikawa H, Finkelstein IJ, Kim S, Kwak K, Chung JK, Wakasugi K, Massari AM, Fayer MD. Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 104: 16116-21. PMID 17916624 DOI: 10.1073/Pnas.0707718104 |
0.775 |
|
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