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Insights into eukaryotic translation initiation factor 5A: Its role and mechanisms in protein synthesis.
Biochim Biophys Acta Mol Cell Res
December 2024
Life Sciences Institute, Zhejiang University, Hangzhou 310058, China. Electronic address:
The protein synthesis within eukaryotic cells is a complex process involving various translation factors. Among these factors, eukaryotic translation initiation factor 5 A (eIF5A) emerges as a crucial translation factor with high evolutionary conservation. eIF5A is unique as it is the only protein in eukaryotic cells containing the hypusine modification.
View Article and Find Full Text PDFDetermining the nanostructure and main axis of gly-his-gly fibrils using the amide I' bands in FTIR, VCD, and Raman spectra.
Spectrochim Acta A Mol Biomol Spectrosc
February 2024
Department of Chemistry, Drexel University, Philadelphia, PA 19104, USA. Electronic address:
The zwitterionic tripeptide glycyl-histidine-glycine (GHG) has been shown to self-assemble into visible crystalline fibrils that form a gel-supporting network with a very high storage modulus. Here we elaborate on the theory and experimental setup behind our novel approach employed to determining the main fibril axis for these gel-forming fibrils by simulating the amide I band profile for infrared absorption (IR), vibrational circular dichroism (VCD), and visible Raman scattering. We also highlight that combining these three vibrational spectroscopies can help in validating structures that are solved using powder x-ray diffraction analysis (PXRD).
View Article and Find Full Text PDFMolecular dynamics simulations of the adsorption of an intrinsically disordered protein: Force field and water model evaluation in comparison with experiments.
Front Mol Biosci
October 2022
Division of Theoretical Chemistry, Lund University, Lund, Sweden.
This study investigates possible structural changes of an intrinsically disordered protein (IDP) when it adsorbs to a solid surface. Experiments on IDPs primarily result in ensemble averages due to their high dynamics. Therefore, molecular dynamics (MD) simulations are crucial for obtaining more detailed information on the atomistic and molecular levels.
View Article and Find Full Text PDFForbidden Secondary Structures Found in Gel-Forming Fibrils of Glycylphenylalanylglycine.
J Phys Chem B
October 2022
Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, Pennsylvania19104, United States.
The zwitterionic l-tripeptide glycylphenylalanylglycine self-assembles into very long crystalline fibrils in an aqueous solution, which causes the formation of an exceptionally strong gel phase (' ∼ 5 × 10 Pa). The Rietveld refinement analysis of its powder X-ray diffraction (PXRD) pattern reveals a unit cell with four peptides forming a 222 space group and adopting an inverse polyproline II conformation, that is, a right-handed helical structure that occupies the "forbidden" region of the Ramachandran plot. This unusual structure is stabilized by a plethora of intermolecular interactions facilitated by the large number of different functional groups of the unblocked tripeptide.
View Article and Find Full Text PDFStructure of the Monkeypox virus profilin-like protein A42R reveals potential functional differences from cellular profilins.
Acta Crystallogr F Struct Biol Commun
October 2022
Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
The infectious disease human monkeypox is spreading rapidly in 2022, causing a global health crisis. The genomics of Monkeypox virus (MPXV) have been extensively analyzed and reported, although little is known about the virus-encoded proteome. In particular, there are no reported experimental MPXV protein structures other than computational models.
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