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Liu, T., Whitten, S. T., Hilser, V. J. (2007) Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proceedings of the National Academy of Sciences, 104 (11) 4347-4352 doi:10.1073/pnas.0607132104

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Reference TypeJournal (article/letter/editorial)
TitleFunctional residues serve a dominant role in mediating the cooperativity of the protein ensemble
JournalProceedings of the National Academy of Sciences
AuthorsLiu, T.Author
Whitten, S. T.Author
Hilser, V. J.Author
Year2007 (March 13)Volume104
Issue11
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0607132104Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1736128Long-form Identifiermindat:1:5:1736128:6
GUID0
Full ReferenceLiu, T., Whitten, S. T., Hilser, V. J. (2007) Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proceedings of the National Academy of Sciences, 104 (11) 4347-4352 doi:10.1073/pnas.0607132104
Plain TextLiu, T., Whitten, S. T., Hilser, V. J. (2007) Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. Proceedings of the National Academy of Sciences, 104 (11) 4347-4352 doi:10.1073/pnas.0607132104
In(2007, March) Proceedings of the National Academy of Sciences Vol. 104 (11) Proceedings of the National Academy of Sciences

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Whitten, S. T., Garcia-Moreno E., B., Hilser, V. J. (2005) Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. Proceedings of the National Academy of Sciences, 102 (12) 4282-4287 doi:10.1073/pnas.0407499102
Hilser, V. J., Thompson, E. B. (2007) Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proceedings of the National Academy of Sciences, 104 (20) 8311-8315 doi:10.1073/pnas.0700329104
Hilser, V. J., Dowdy, D., Oas, T. G., Freire, E. (1998) The structural distribution of cooperative interactions in proteins: Analysis of the native state ensemble. Proceedings of the National Academy of Sciences, 95 (17) 9903-9908 doi:10.1073/pnas.95.17.9903
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Liu, S., Liu, S., Zhu, X., Liang, H., Cao, A., Chang, Z., Lai, L. (2007) Nonnatural protein-protein interaction-pair design by key residues grafting. Proceedings of the National Academy of Sciences, 104 (13) 5330-5335 doi:10.1073/pnas.0606198104
Qi, X., Portman, J. J. (2007) Excluded volume, local structural cooperativity, and the polymer physics of protein folding rates. Proceedings of the National Academy of Sciences, 104 (26) 10841-10846 doi:10.1073/pnas.0609321104
Morita, T., Aiba, H. (2007) Small RNAs making a small protein. Proceedings of the National Academy of Sciences, 104 (51) 20149-20150 doi:10.1073/pnas.0710634105
Hughes, A. D., Anslyn, E. V. (2007) A cationic host displaying positive cooperativity in water. Proceedings of the National Academy of Sciences, 104 (16) 6538-6543 doi:10.1073/pnas.0609144104
Huiskonen, J. T., Manole, V., Butcher, S. J. (2007) Tale of two spikes in bacteriophage PRD1. Proceedings of the National Academy of Sciences, 104 (16) 6666-6671 doi:10.1073/pnas.0608625104
Tang, J., Sawasdikosol, S., Chang, J.-H., Burakoff, S. J. (1999) SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling. Proceedings of the National Academy of Sciences, 96 (17) 9775-9780 doi:10.1073/pnas.96.17.9775
Shi, H., Fan, X., Sevilimedu, A., Lis, J. T. (2007) RNA aptamers directed to discrete functional sites on a single protein structural domain. Proceedings of the National Academy of Sciences, 104 (10) 3742-3746 doi:10.1073/pnas.0607805104
 
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