Skip to main content
Article thumbnail
Location of Repository

Protein Dynamics: From Molecules, to Interactions, to Biology

By Martin Gruebele

Abstract

Proteins have a remarkably rich diversity of dynamical behaviors, and the articles in this issue of the International Journal of Molecular Sciences are a testament to that fact. From the picosecond motions of single sidechains probed by NMR or fluorescence spectroscopy, to aggregation processes at interfaces that take months, all time scales play a role. Proteins are functional molecules, so by their nature they always interact with their environment. This environment includes water, other biomolecules, or larger cellular structures. In a sense, it also includes the protein molecule itself: proteins are large enough to fold and interact with themselves. These interactions have been honed by evolution to produce behaviors completely different from those of random polymers

Topics: Editorial
Publisher: Molecular Diversity Preservation International (MDPI)
OAI identifier: oai:pubmedcentral.nih.gov:2672034
Provided by: PubMed Central
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://www.pubmedcentral.nih.g... (external link)
  • Suggested articles

    Citations

    1. (2002). A view of the hydrophobic effect.
    2. (2008). An experimental survey of the transition between two-state and downhill protein folding scenarios.
    3. (2009). Caging helps proteins fold.
    4. (2001). Chaperonin-mediated protein folding.
    5. (2005). Downhill protein folding: evolution meets physics.
    6. (2002). Experimental identification of downhill protein folding. Science
    7. (2003). Folding at the speed limit.
    8. (1989). Intermediates and barrier crossing in random energy model (with applications to protein folding).
    9. (2005). Mass fractal dimension and the compactness of proteins.
    10. (1995). Molecular chaperones in cellular protein folding.
    11. (2006). Nanosecond folding dynamics of a three-stranded beta-sheet.
    12. (2001). NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry
    13. (1999). Observation of strange kinetics in protein folding.
    14. (1997). Parallel tempering algorithm for conformational studies of biological molecules.
    15. (1995). pathways, and the energy landscape of protein folding: A synthesis.
    16. (1999). Polymer principles and protein folding. Protein Sci.
    17. Principles that govern the folding of protein chains.
    18. (2003). Protein folding and misfolding.
    19. (2008). Protein sequence- and pH-dependent hydration probed by Terahertz spectroscopy.
    20. (2002). Solvent fluctuations dominate protein dynamics and functions.
    21. (2000). Speeding molecular recognition by using the folding funnel: The fly-casting mechanism.
    22. (1993). Structure and functional complementation of engineered fragments from yeast phosphoglycerate kinase.
    23. (2008). Ten-microsecond molecular dynamics simulation of a fast-folding WW domain.
    24. (2008). Terahertz absorption as a new probe of solvation structure during protein folding kinetics.
    25. (1999). The fast protein folding problem.
    26. (2004). The protein folding 'speed limit'.
    27. (1983). Theoretical studies of protein folding.
    28. (2003). Trp-cage: Folding free energy landscape in explicit water.
    29. (2003). Tuning the heterogeneous early folding dynamics of phosphoglycerate kinase.
    30. (2002). What does it mean to be natively unfolded?

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.