ArticleJournal of biological physics2012
Role of methyl groups in dynamics and evolution of biomolecules.
Article in Journal of biological physics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Article
- The effect of a methyl group on structure and function: Serine vs. threonine glycosylation and phosphorylation.Frontiers in molecular biosciences · 2023Review
- Low rotational barriers for the most dynamically active methyl groups in the proposed antiviral drugs for treatment of SARS-CoV-2, apilimod and tetrandrine.Chemical physics letters · 2021Article
- Article
- Water in protein hydration and ligand recognition.Journal of molecular recognition : JMR · 2019Review
- Structural effects of modified ribonucleotides and magnesium in transfer RNAs.Bioorganic & medicinal chemistry · 2016Article
- Coherent neutron scattering and collective dynamics in the protein, GFP.Biophysical journal · 2013Article
- Dynamics of protein and its hydration water: neutron scattering studies on fully deuterated GFP.Biophysical journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies have discovered strong differences between the dynamics of nucleic acids (RNA and DNA) and proteins, especially at low hydration and low temperatures. This difference is caused primarily by dynamics of methyl groups that are abundant in proteins, but are absent or very rare in RNA and DNA. In this paper, we present a hypothesis regarding the role of methyl groups as intrinsic plasticizers in proteins and their evolutionary selection to facilitate protein dynamics and activity. We demonstrate the profound effect methyl groups have on protein dynamics relative to nucleic acid dynamics, and note the apparent correlation of methyl group content in protein classes and their need for molecular flexibility. Moreover, we note the fastest methyl groups of some enzymes appear around dynamical centers such as hinges or active sites. Methyl groups are also of tremendous importance from a hydrophobicity/folding/entropy perspective. These significant roles, however, complement our hypothesis rather than preclude the recognition of methyl groups in the dynamics and evolution of biomolecules.Electronic supplementary material The online version of this article (doi:10.1007/s10867-012-9268-6) contains supplementary material, which is available to authorized users.
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Registered trials
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