Review
doi: 10.1038/nature06522.
Dynamic personalities of proteins
Affiliations
- PMID: 18075575
- DOI: 10.1038/nature06522
Item in Clipboard
Review
Dynamic personalities of proteins
Nature.
.
Abstract
Because proteins are central to cellular function, researchers have sought to uncover the secrets of how these complex macromolecules execute such a fascinating variety of functions. Although static structures are known for many proteins, the functions of proteins are governed ultimately by their dynamic character (or 'personality'). The dream is to 'watch' proteins in action in real time at atomic resolution. This requires addition of a fourth dimension, time, to structural biology so that the positions in space and time of all atoms in a protein can be described in detail.
Similar articles
-
Physicochemical bases for protein folding, dynamics, and protein-ligand binding.Sci China Life Sci. 2014 Mar;57(3):287-302. doi: 10.1007/s11427-014-4617-2. Epub 2014 Feb 19. Sci China Life Sci. 2014. PMID: 24554472 Review.
-
Bridging from molecular simulation to biochemical networks.Curr Opin Struct Biol. 2007 Apr;17(2):166-72. doi: 10.1016/j.sbi.2007.03.014. Epub 2007 Mar 28. Curr Opin Struct Biol. 2007. PMID: 17395455 Review.
-
Uncovering protein structure.Essays Biochem. 2020 Oct 8;64(4):649-680. doi: 10.1042/EBC20190042. Essays Biochem. 2020. PMID: 32975287 Free PMC article. Review.
-
Combining molecular dynamics and machine learning to improve protein function recognition.Pac Symp Biocomput. 2008:332-43. Pac Symp Biocomput. 2008. PMID: 18229697 Free PMC article.
-
Picosecond time-resolved X-ray crystallography: probing protein function in real time.J Struct Biol. 2004 Sep;147(3):235-46. doi: 10.1016/j.jsb.2004.06.009. J Struct Biol. 2004. PMID: 15450293
Cited by
-
Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods. 2021 Sep;193:116-135. doi: 10.1016/j.ymeth.2021.03.018. Epub 2021 Apr 6. Methods. 2021. PMID: 33831596 Free PMC article.
-
Multiquantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.J Phys Chem Lett. 2020 Jul 16;11(14):5649-5654. doi: 10.1021/acs.jpclett.0c01322. Epub 2020 Jul 2. J Phys Chem Lett. 2020. PMID: 32543198 Free PMC article.
-
Transition States and transition state analogue interactions with enzymes.Acc Chem Res. 2015 Apr 21;48(4):1032-9. doi: 10.1021/acs.accounts.5b00002. Epub 2015 Apr 7. Acc Chem Res. 2015. PMID: 25848811 Free PMC article.
-
The dynamics of the G protein-coupled neuropeptide Y2 receptor in monounsaturated membranes investigated by solid-state NMR spectroscopy.J Biomol NMR. 2015 Apr;61(3-4):347-59. doi: 10.1007/s10858-014-9892-5. Epub 2015 Jan 6. J Biomol NMR. 2015. PMID: 25556885
-
Substrate Binding Stiffens Aspartate Aminotransferase by Altering the Enzyme Picosecond Vibrational Dynamics.ACS Omega. 2020 Jul 23;5(30):18787-18797. doi: 10.1021/acsomega.0c01900. eCollection 2020 Aug 4. ACS Omega. 2020. PMID: 32775880 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
