A review of the recent data on protein dynamics (mainly myoglobin) by X-ray technique, Mössbauer spectroscopy and Rayleigh scattering of Mössbauer radiation is given. The connection between dynamical and functional properties of biological systems are discussed.
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ACS Chem Neurosci
January 2025
School of Health & Life Sciences, Teesside University, Middlesbrough TS1 3BX, United Kingdom.
The aggregation of α-synuclein is crucial to the development of Lewy body diseases, including Parkinson's disease and dementia with Lewy bodies. The aggregation pathway of α-synuclein typically involves a defined sequence of nucleation, elongation, and secondary nucleation, exhibiting prion-like spreading. This study employed Raman spectroscopy and machine learning analysis, alongside complementary techniques, to characterize the biomolecular changes during the fibrillation of purified recombinant wild-type α-synuclein protein.
View Article and Find Full Text PDFPlant Physiol
December 2024
Department of Biology, University of Oxford, South Parks Road, Oxford OX1 3RB, UK.
The cysteine/arginine (Cys/Arg) branch of the N-degron pathway controls the stability of certain proteins with methionine (Met)-Cys N-termini, initiated by Met cleavage and Cys oxidation. In seeding plants, target proteins include the Group VII Ethylene Response Factors, which initiate adaptive responses to low oxygen (hypoxic) stress, as well as Vernalization 2 (VRN2) and Little Zipper 2 (ZPR2), which are involved in responses to endogenous developmental hypoxia. It is essential that these target proteins are only degraded by the N-degron pathway under the appropriate physiological conditions.
View Article and Find Full Text PDFTrends Biochem Sci
January 2025
Department of Chemistry, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-Ku, Kyoto 606-8502, Japan; Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Yoshida-Ushinomiyacho, Sakyo-Ku, Kyoto 606-8501, Japan. Electronic address:
DNA can fold into noncanonical left-handed Z-DNA conformation beyond the right-handed B-DNA. While its crystal structure was discovered nearly four decades ago, it was predominantly considered a structural curiosity. Recent evidence suggests that Z-DNA formation occurs in nuclear and mitochondrial DNA (mtDNA), with significant biological implications.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
The microbial aminotransferase enzyme DapC is vital for lysine biosynthesis in various Gram-positive bacteria, including . Characterization of the enzyme's conformational dynamics and identifying the key residues for ligand binding are crucial for the development of effective antimicrobials. This study employs atomistic simulations to explore and categorize the dynamics of DapC in comparison to other classes of aminotransferase.
View Article and Find Full Text PDFPLoS Comput Biol
January 2025
Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou, Zhejiang, China.
In eukaryotes, DNA achieves a highly compact structure primarily due to its winding around the histone cores. The nature wrapping of DNA around histone core form a 1.7 left-handed superhelical turns, contributing to negative supercoiling in chromatin.
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