Quantum mechanics simulation of protein dynamics on long timescale - PubMed (original) (raw)
. 2001 Sep 1;44(4):484-9.
doi: 10.1002/prot.1114.
Affiliations
- PMID: 11484226
- DOI: 10.1002/prot.1114
Quantum mechanics simulation of protein dynamics on long timescale
H Liu et al. Proteins. 2001.
Abstract
Protein structure and dynamics are the keys to a wide range of problems in biology. In principle, both can be fully understood by using quantum mechanics as the ultimate tool to unveil the molecular interactions involved. Indeed, quantum mechanics of atoms and molecules have come to play a central role in chemistry and physics. In practice, however, direct application of quantum mechanics to protein systems has been prohibited by the large molecular size of proteins. As a consequence, there is no general quantum mechanical treatment that not only exceeds the accuracy of state-of-the-art empirical models for proteins but also maintains the efficiency needed for extensive sampling in the conformational space, a requirement mandated by the complexity of protein systems. Here we show that, given recent developments in methods, a general quantum mechanical-based treatment can be constructed. We report a molecular dynamics simulation of a protein, crambin, in solution for 350 ps in which we combine a semiempirical quantum-mechanical description of the entire protein with a description of the surrounding solvent, and solvent-protein interactions based on a molecular mechanics force field. Comparison with a recent very high-resolution crystal structure of crambin (Jelsch et al., Proc Natl Acad Sci USA 2000;102:2246-2251) shows that geometrical detail is better reproduced in this simulation than when several alternate molecular mechanics force fields are used to describe the entire system of protein and solvent, even though the structure is no less flexible. Individual atomic charges deviate in both directions from "canonical" values, and some charge transfer is found between the N and C-termini. The capability of simulating protein dynamics on and beyond the few hundred ps timescale with a demonstrably accurate quantum mechanical model will bring new opportunities to extend our understanding of a range of basic processes in biology such as molecular recognition and enzyme catalysis.
Copyright 2001 Wiley-Liss, Inc.
Similar articles
- A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations.
Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, Zhang W, Yang R, Cieplak P, Luo R, Lee T, Caldwell J, Wang J, Kollman P. Duan Y, et al. J Comput Chem. 2003 Dec;24(16):1999-2012. doi: 10.1002/jcc.10349. J Comput Chem. 2003. PMID: 14531054 - Molecular dynamics and quantum mechanics of RNA: conformational and chemical change we can believe in.
Ditzler MA, Otyepka M, Sponer J, Walter NG. Ditzler MA, et al. Acc Chem Res. 2010 Jan 19;43(1):40-7. doi: 10.1021/ar900093g. Acc Chem Res. 2010. PMID: 19754142 Free PMC article. - First-principles-based multiscale, multiparadigm molecular mechanics and dynamics methods for describing complex chemical processes.
Jaramillo-Botero A, Nielsen R, Abrol R, Su J, Pascal T, Mueller J, Goddard WA 3rd. Jaramillo-Botero A, et al. Top Curr Chem. 2012;307:1-42. doi: 10.1007/128_2010_114. Top Curr Chem. 2012. PMID: 21243466 Review. - Free energies of chemical reactions in solution and in enzymes with ab initio quantum mechanics/molecular mechanics methods.
Hu H, Yang W. Hu H, et al. Annu Rev Phys Chem. 2008;59:573-601. doi: 10.1146/annurev.physchem.59.032607.093618. Annu Rev Phys Chem. 2008. PMID: 18393679 Free PMC article. Review.
Cited by
- Drug screening of α-amylase inhibitors as candidates for treating diabetes.
Alp M, Misturini A, Sastre G, Gálvez-Llompart M. Alp M, et al. J Cell Mol Med. 2023 Aug;27(15):2249-2260. doi: 10.1111/jcmm.17831. Epub 2023 Jul 4. J Cell Mol Med. 2023. PMID: 37403218 Free PMC article. - Variational consistent histories as a hybrid algorithm for quantum foundations.
Arrasmith A, Cincio L, Sornborger AT, Zurek WH, Coles PJ. Arrasmith A, et al. Nat Commun. 2019 Jul 31;10(1):3438. doi: 10.1038/s41467-019-11417-0. Nat Commun. 2019. PMID: 31366888 Free PMC article. - Analysis of Phosphoryl-Transfer Enzymes with QM/MM Free Energy Simulations.
Roston D, Lu X, Fang D, Demapan D, Cui Q. Roston D, et al. Methods Enzymol. 2018;607:53-90. doi: 10.1016/bs.mie.2018.05.005. Epub 2018 Aug 14. Methods Enzymol. 2018. PMID: 30149869 Free PMC article. - Elucidating the fundamental forces in protein crystal formation: the case of crambin.
Delle Piane M, Corno M, Orlando R, Dovesi R, Ugliengo P. Delle Piane M, et al. Chem Sci. 2016 Feb 1;7(2):1496-1507. doi: 10.1039/c5sc03447g. Epub 2015 Nov 24. Chem Sci. 2016. PMID: 29899894 Free PMC article. - Diverse effects of distance cutoff and residue interval on the performance of distance-dependent atom-pair potential in protein structure prediction.
Yao Y, Gui R, Liu Q, Yi M, Deng H. Yao Y, et al. BMC Bioinformatics. 2017 Dec 8;18(1):542. doi: 10.1186/s12859-017-1983-3. BMC Bioinformatics. 2017. PMID: 29221443 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials