Dynamic personalities of proteins
- PMID: 18075575
- DOI: 10.1038/nature06522
Dynamic personalities of proteins
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
-
A unified view on enzyme catalysis by cryo-EM study of a DNA topoisomerase.Commun Chem. 2024 Feb 28;7(1):45. doi: 10.1038/s42004-024-01129-y. Commun Chem. 2024. PMID: 38418525 Free PMC article.
-
Functional analysis of single enzymes combining programmable molecular circuits with droplet-based microfluidics.Nat Nanotechnol. 2024 Feb 26. doi: 10.1038/s41565-024-01617-1. Online ahead of print. Nat Nanotechnol. 2024. PMID: 38409552
-
Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development.ACS Omega. 2024 Feb 8;9(7):7393-7412. doi: 10.1021/acsomega.3c09084. eCollection 2024 Feb 20. ACS Omega. 2024. PMID: 38405524 Free PMC article. Review.
-
Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.Proc Natl Acad Sci U S A. 2024 Feb 27;121(9):e2313192121. doi: 10.1073/pnas.2313192121. Epub 2024 Feb 22. Proc Natl Acad Sci U S A. 2024. PMID: 38386706 Free PMC article.
-
A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Appl Magn Reson. 2024;55(1-3):251-277. doi: 10.1007/s00723-023-01618-8. Epub 2023 Oct 14. Appl Magn Reson. 2024. PMID: 38357006 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
