DOI: 10.1038/nsmb739. Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation

Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation

10.1038/nsmb739

Crossref journal-article

Springer Science and Business Media LLC

Nature Structural & Molecular Biology (297)

Bibliography

Babu, C. R., Hilser, V. J., & Wand, A. J. (2004). Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation. Nature Structural & Molecular Biology, 11(4), 352â357.

Authors 3

Charles R Babu (first)
Vincent J Hilser (additional)
A Joshua Wand (additional)

References 21 Referenced 128

Privalov, P.L. Cold denaturation of proteins. Crit. Rev. Biochem. Mol. Biol. 25, 281–305 (1990). (10.3109/10409239009090612) / Crit. Rev. Biochem. Mol. Biol. by PL Privalov (1990)
Nash, D.P. & Jonas, J. Structure of the pressure-assisted cold denatured state of ubiquitin. Biochem. Biophys. Res. Comm. 238, 289–291 (1997). (10.1006/bbrc.1997.7308) / Biochem. Biophys. Res. Comm. by DP Nash (1997)
Bai, Y., Sosnick, T.R., Mayne, L. & Englander, S.W. Protein folding intermediates: native-state hydrogen exchange. Science 269, 192–197 (1995). (10.1126/science.7618079) / Science by Y Bai (1995)
Fuentes, E.J. & Wand, A.J. Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37, 9877–9883 (1998). (10.1021/bi980894o) / Biochemistry by EJ Fuentes (1998)
Hatley, R.H.M. & Franks, F. The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants. FEBS Lett. 257, 171–173 (1989). (10.1016/0014-5793(89)81813-7) / FEBS Lett. by RHM Hatley (1989)
Wand, A.J., Ehrhardt, M.R. & Flynn, P.F. High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Proc. Natl. Acad. Sci. USA 95, 15299–15302 (1998). (10.1073/pnas.95.26.15299) / Proc. Natl. Acad. Sci. USA by AJ Wand (1998)
Babu, C.R., Flynn, P.F. & Wand, A.J. Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids. J. Am. Chem. Soc. 123, 2691–2692 (2001). (10.1021/ja005766d) / J. Am. Chem. Soc. by CR Babu (2001)
Wintrode, P.L., Makhatadze, G.I. & Privalov, P.L. Thermodynamics of ubiquitin unfolding. Proteins 18, 246–253 (1994). (10.1002/prot.340180305) / Proteins by PL Wintrode (1994)
Ibarra-Molero, B., Makhatadze, G.I. & Sanchez-Ruiz, J.M. Cold denaturation of ubi-quitin. Biochim. Biophys. Acta 1429, 384–390 (1999). (10.1016/S0167-4838(98)00252-0) / Biochim. Biophys. Acta by B Ibarra-Molero (1999)
Skalicky, J.J., Sukumaran, D.K., Mills, J.L. & Szyperski, T. Toward structural biology in supercooled water. J. Am. Chem. Soc. 122, 3230–3231 (2000). (10.1021/ja9938884) / J. Am. Chem. Soc. by JJ Skalicky (2000)
Zhou, H.X. & Dill, K.A. Stabilization of proteins in confined spaces. Biochemistry 40, 11289–11293 (2001). (10.1021/bi0155504) / Biochemistry by HX Zhou (2001)
Shastry, M.C.R. & Eftink, M.R. Reversible thermal unfolding of ribonuclease T1 in reverse micelles. Biochemistry 35, 4094–4101 (1996). (10.1021/bi952550t) / Biochemistry by MCR Shastry (1996)
Battistel, E., Luisi, P.L. & Rialdi, G. Thermodynamic study of globular protein stability in microemulsions. J. Phys. Chem. 92, 6680–6685 (1988). (10.1021/j100334a038) / J. Phys. Chem. by E Battistel (1988)
Dill, K.A., Fiebig, K.M. & Chan, H.S. Cooperativity in protein-folding kinetics. Proc. Natl. Acad. Sci. USA 90, 1942–1946 (1993). (10.1073/pnas.90.5.1942) / Proc. Natl. Acad. Sci. USA by KA Dill (1993)
Sivaraman, T., Arrington, C.B. & Robertson, A.D. Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin. Nat. Struct. Biol. 8, 331–331 (2001). (10.1038/86208) / Nat. Struct. Biol. by T Sivaraman (2001)
Briggs, M.S. & Roder, H. Proc. Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc. Natl. Acad. Sci. USA 89, 2017–2021 (1992). (10.1073/pnas.89.6.2017) / Proc. Natl. Acad. Sci. USA by MS Briggs (1992)
Shortle, D. & Ackerman, M.S. Persistence of native-like topology in a denatured protein in 8 M urea. Science 293, 487–489 (2001) (10.1126/science.1060438) / Science by D Shortle (2001)
Hilser, V.J. & Freire, E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J. Mol. Biol. 262, 756–772 (1996). (10.1006/jmbi.1996.0550) / J. Mol. Biol. by VJ Hilser (1996)
Hilser, V.J., Dowdy, D., Oas, T. & Freire, E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc. Natl. Acad. Sci. USA 95, 9903–9908 (1998). (10.1073/pnas.95.17.9903) / Proc. Natl. Acad. Sci. USA by VJ Hilser (1998)
Ooi, T. & Oobatake, M. Prediction of the thermodynamics of protein unfolding: the helix-coil transition of poly(L-alanine). Proc. Natl. Acad. Sci. USA 88, 2859–2863 (1991). (10.1073/pnas.88.7.2859) / Proc. Natl. Acad. Sci. USA by T Ooi (1991)
Wand, A.J., Urbauer, J.L., McEvoy, R.P. & Bieber, R.J. Internal dynamics of human ubiquitin revealed by 13C-relaxation of randomly, fractionally enriched protein. Biochemistry 35, 6116–6125 (1996). (10.1021/bi9530144) / Biochemistry by AJ Wand (1996)

Dates

Type	When
Created	21 years, 5 months ago (Feb. 29, 2004, 1:45 p.m.)
Deposited	2 years, 3 months ago (May 19, 2023, 12:52 a.m.)
Indexed	3 days, 21 hours ago (Aug. 23, 2025, 9:43 p.m.)
Issued	21 years, 5 months ago (Feb. 29, 2004)
Published	21 years, 5 months ago (Feb. 29, 2004)
Published Online	21 years, 5 months ago (Feb. 29, 2004)
Published Print	21 years, 4 months ago (April 1, 2004)

Funders 0

None

BibTeX

@article{Babu_2004, title={Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation}, volume={11}, ISSN={1545-9985}, url={http://dx.doi.org/10.1038/nsmb739}, DOI={10.1038/nsmb739}, number={4}, journal={Nature Structural & Molecular Biology}, publisher={Springer Science and Business Media LLC}, author={Babu, Charles R and Hilser, Vincent J and Wand, A Joshua}, year={2004}, month=feb, pages={352–357} }

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