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Hydrogen bonding stabilizes globular proteins
Open accessAbstract
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globular proteins. It is not clear, however, whether they make a net favorable contribution to this stability. Experimental and theoretical studies are at odds over this important question. Measurements of the change in conformational stability, delta (delta G), for the mutation of a hydrogen bonded residue to one incapable of hydrogen bonding suggest a stabilization of 1.0 kcal/mol per hydrogen bond. If the delta (delta G) values are corrected for differences in side-chain hydrophobicity and conformational entropy, then the estimated stabilization becomes 2.2 kcal/mol per hydrogen bond. These and other experimental studies discussed here are consistent and compelling: hydrogen bonding stabilizes globular proteins.
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“Polyester systems can interact due to hydrophilic, hydrophobic, and electrostatic interactions such as dipole-dipole interactions [41], but they lack the ability to form regular repeating intramolecular hydrogen bonding motifs of the sort that facilitate protein folding [42,43].”
From Polyesters as a Model System for Building Primitive Biologies from Non-Biological Prebiotic Chemistry (2020) · cites this paper as [43]
Citations
Cites
Some Factors in the Interpretation of Protein Denaturation
Kauzmann, W. (1959) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60608-7 · Cited by 4,880
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
The Hydrophobic Effect: Formation of Micelles and Biological Membranes
Tanford, C. (1991) · Medical Entomology and Zoology · Cited by 3,327
AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTURE
Richards, F. M. (1977) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.06.060177.001055 · Cited by 2,660
Satisfying Hydrogen Bonding Potential in Proteins
McDonald, I. K., & Thornton, J. M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1334 · Cited by 2,136
Hydrogen bonding in globular proteins
Baker, E. N., & Hubbard, R. E. (1984) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(84)90007-5 · Cited by 1,860
Energetics of Protein Structure
Makhatadze, G. I., & Privalov, P. L. (1995) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60548-3 · Cited by 1,073
Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins
Tanford, C. (1962) · Journal of the American Chemical Society · doi:10.1021/ja00881a009 · Cited by 1,016
Sauer-Eriksson, A. E., Baase, W. A., Zhang, X. ‐., Heinz, D. W., Blaber, M., Baldwin, E. P., & Matthews, B. W. (1992) · Science · doi:10.1126/science.1553543 · Cited by 920
Elucidating the folding problem of helical peptides using empirical parameters
Muñoz, V., & Serrano, L. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0694-399 · Cited by 721
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Mitra, N. K., Srinivas, V. R., Ramya, T. N. C., Ahmad, N., Reddy, G. B., & Surolia, A. (2002) · Biochemistry · doi:10.1021/bi020240m · Cited by 41
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Yang, Y., Ding, X., Zhu, G., Niroula, A., Lv, Q., & Vihinen, M. (2019) · BMC Genomics · doi:10.1186/s12864-019-6138-7 · Cited by 40
Efimov, A. V., & Бражников, Е. В. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01189-x · Cited by 40
Ishak, S. N. H., Aris, S. N. A. M., Halim, K. B. A., Ali, M. S. M., Leow, T. C., Kamarudin, N. H. A., Masomian, M., & Rahman, R. N. Z. R. A. (2017) · Molecules · doi:10.3390/molecules22101574 · Cited by 39
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Kim, D., Jang, D. S., Nam, G. H., Choi, G., Kim, J.-S., Ha, N., Kim, M., Oh, B., & Choi, K. Y. (2000) · Biochemistry · doi:10.1021/bi992119u · Cited by 39
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Pal, P., Chakraborty, S., & Jana, B. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c05367 · Cited by 37
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Irún, P., Maldonado, S., & Sancho, J. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.3.173 · Cited by 37
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Takano, K., Ota, M., Ogasahara, K., Yamagata, Y., Nishikawa, K., & Yutani, K. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.8.663 · Cited by 35
Gong, H., Shen, Y., & Rose, G. D. (2007) · Protein Science · doi:10.1110/ps.072988407 · Cited by 35
Goswami, S., Das, S., & Datta, S. (2017) · Protein Engineering Design and Selection · doi:10.1093/protein/gzx039 · Cited by 34
Peterson, R. W., Nicholson, E. M., Thapar, R., Klevit, R. E., & Scholtz, J. M. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2574 · Cited by 34
Leverentz, H. R., & Truhlar, D. G. (2008) · The Journal of Physical Chemistry A · doi:10.1021/jp8018364 · Cited by 33
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Royo, M., Daubner, S. C., & Fitzpatrick, P. F. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20293 · Cited by 31
Zhu, H., Celinski, S. A., Scholtz, J. M., & Hu, J. C. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3936 · Cited by 31
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Laurents, D. V., Pérez‐Cañadillas, J. M., Santoro, J., Rico, M., Schell, D., Pace, C. N., & Bruix, M. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1085 · Cited by 30
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Yang, J. H., Park, J. Y., Kim, S. H., & Yoo, Y. J. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2007.10.008 · Cited by 29
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Lakshminarayanan, R., Bromley, K. M., Lei, Y., Snead, M. L., & Moradian‐Oldak, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.131136 · Cited by 29
Quantification of helix–helix binding affinities in micelles and lipid bilayers
Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2004) · Protein Science · doi:10.1110/ps.04850804 · Cited by 29
Duan, L. L., Gao, Y., Mei, Y., Zhang, Q. G., Tang, B., & Zhang, J. Z. H. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp212516g · Cited by 28
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Yuan, C., Byeon, I. L., Li, Y., & Tsai, M. (1999) · Biochemistry · doi:10.1021/bi982211a · Cited by 27
Berezovsky, I. N., Namiot, V. A., Tumanyan, V. G., & Ng, E. (1999) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1999.10508347 · Cited by 27
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Zhu, S. N., & Elcock, A. H. (2010) · Journal of Chemical Theory and Computation · doi:10.1021/ct1000704 · Cited by 25
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Kim, D.-J., Kim, Y., Kim, A.-D., & Jeong, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114160 · Cited by 24
Kaushik, J. K., Iimura, S., Ogasahara, K., Yamagata, Y., Segawa, S.-I., & Yutani, K. (2006) · Biochemistry · doi:10.1021/bi052610n · Cited by 24
Blomberg, E., Kumpulainen, A. J., David, C., & Amiel, C. (2004) · Langmuir · doi:10.1021/la048370e · Cited by 25
Baldwin, R. L. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch6 · Cited by 25
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Cao, Z., & Bowie, J. U. (2014) · Protein Science · doi:10.1002/pro.2435 · Cited by 20
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DasGupta, D., Mandalaparthy, V., & Jayaram, B. (2017) · Journal of Computational Chemistry · doi:10.1002/jcc.25072 · Cited by 24
Xiao, J., Melvin, R. L., & Salsbury, F. R. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1445032 · Cited by 20
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Aharoni, A., & Horovitz, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1698 · Cited by 20
Yang, X.-Y., Kathuria, S. V., Vadrevu, R., & Matthews, C. R. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007179 · Cited by 19
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Song, Z., Zheng, X., & Yang, B. (2013) · Protein Science · doi:10.1002/pro.2338 · Cited by 19
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Arumugam, K., & Crouzy, S. (2012) · Biochemistry · doi:10.1021/bi300669e · Cited by 18
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Alajmi, M. F., Khan, S., Choudhury, A., Mohammad, T., Noor, S., Hussain, A., Lu, W., Eapen, M. S., Chimankar, V., Hansbro, P. M., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.780284 · Cited by 17
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Diaconu, A., Nita, L. E., Chiriac, A. P., & Butnaru, M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.08.033 · Cited by 16
WALLACE, L. A., Blatch, G. L., & Dirr, H. W. (1998) · Biochemical Journal · doi:10.1042/bj3360413 · Cited by 16
Chatterjee, S., Salimi, A., & Lee, J. Y. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp00105a · Cited by 15
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Baker, B. M., Ding, Y., Garboczi, D. N., Biddison, W. E., & Wiley, D. C. (1999) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1999.64.235 · Cited by 15
Yu, J., Zhang, T., Xu, H., Dong, X., Cai, Y., Pan, Y., & Cao, C. (2019) · RSC Advances · doi:10.1039/c9ra07397c · Cited by 14
Singh, R., Dar, T. A., Ahmad, S., Moosavi‐Movahedi, A. A., & Ahmad, F. (2007) · Biophysical Chemistry · doi:10.1016/j.bpc.2007.12.006 · Cited by 14
Balakrishnan, S., & Sarma, S. P. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00437 · Cited by 14
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Ross, N. T., & Miller, B. L. (2007) · Protein Science · doi:10.1110/ps.073128607 · Cited by 14
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Soriano‐Correa, C., del Valle, F. J. O., Muñoz‐Losa, A., Galván, I. F., Martín, M. E., & Aguilar, M. A. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp1035162 · Cited by 13
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Metadata
- Authors
- Myers, J. K., & Pace, C. N.
- Affiliations
- Texas A&M University (US)
- ORCID
- Pace, C.N.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 1996-10
- Volume
- 71
- Issue
- 4
- Pages
- 2033-2039
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC1233669
- OpenAlex
- W2025925640
- Cited by
- 308
- References
- 74
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 11 · 2022: 12 · 2021: 8 · 2020: 8 · 2019: 7 · 2018: 9 · 2017: 11 · 2016: 11 · 2015: 8 · 2014: 11 · 2013: 8 · 2012: 8
- FWCI
- 4.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM008523, GM37039, T32 GM 08523, R01GM037039)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Crystallography and molecular interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- hydrogen bonding, protein stability, globular proteins, intramolecular hydrogen bonding, conformational stability, side chain hydrophobicity, conformational entropy
- MeSH terms
- Calorimetry, Hydrogen Bonding, Micrococcal Nuclease, Models, Theoretical, Muramidase, Protein Conformation, Protein Denaturation, Proteins, Recombinant Proteins, Thermodynamics, Mutagenesis, Site-Directed, Bacteriophage T4, Point Mutation
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