Irradiation effects on secondary structure of protein induced by keV ions

Cui, Fuzhai; Lin, Y.B.; Zhang, D.M.; Tian, M. B.

doi:10.1016/s0969-806x(00)00341-8

Cited by 14 publications

(8 citation statements)

References 21 publications

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“…40 Many theoretical and experimental studies have been conducted to correlate IR absorption bands of proteins to their secondary structure content, based on the spectra of the proteins either in the solid state or in aqueous solution. 33,[40][41][42] Table 2 represents the peak position and analyzed data obtained from FTIR spectroscopy. The positions of peaks are in agreement with findings of other authors.…”

Section: Resultsmentioning

confidence: 99%

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)

2006

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Secondary structural changes and partitioning process of bovine serum albumin (BSA) in the mixture of (poly-(ethylene glycol 2000) + K 2 HPO 4 + H 2 O) have been studied at 23°C. The effect of varying weight percents of poly(ethylene glycol) and K 2 HPO 4 on the secondary structure of partitioned BSA and the partitioning process of BSA were examined. The equilibrium weight percents of the obtained aqueous two-phase system (ATPS) have been evaluated, and the phase diagrams including the tie lines are presented. It was found that the magnitude of the partition coefficient of BSA and the secondary structures of partitioned BSA depend on the length of obtained tie lines. Occurrences of changes on the secondary structure content of the partitioned BSA were observed by FTIR spectroscopy investigation. The amounts of the secondary structure content of partitioned BSA as R-helix, -sheet, -turn, and unordered structures of BSA were determined and reported.

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Section: Resultsmentioning

confidence: 99%

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)

2006

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“…The putative role of one or several proteins in nanon propagation is also supported by the inhibitory effects of gamma or UV irradiation. Indeed, exposure of proteic molecules to these treatments can provoke secondary conformational changes of proteins which alter their functional properties in turn [ 16 ]. This hypothesis was emphasized by the inhibitory activity of trypsin evidenced here for the first time.…”

Section: Discussionmentioning

confidence: 99%

Nanobacteria Are Mineralo Fetuin Complexes

et al. 2008

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“Nanobacteria” are nanometer-scale spherical and ovoid particles which have spurred one of the biggest controversies in modern microbiology. Their biological nature has been severely challenged by both geologists and microbiologists, with opinions ranging from considering them crystal structures to new life forms. Although the nature of these autonomously replicating particles is still under debate, their role in several calcification-related diseases has been reported. In order to gain better insights on this calciferous agent, we performed a large-scale project, including the analysis of “nanobacteria” susceptibility to physical and chemical compounds as well as the comprehensive nucleotide, biochemical, proteomic, and antigenic analysis of these particles. Our results definitively ruled out the existence of “nanobacteria” as living organisms and pointed out the paradoxical role of fetuin (an anti-mineralization protein) in the formation of these self-propagating mineral complexes which we propose to call “nanons.” The presence of fetuin within renal calculi was also evidenced, suggesting its role as a hydroxyapatite nucleating factor.

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“…[62] It was attributedt oc rosslinking,b ut might also be due to conformational change. Indeed, ap rogressive transition from an a-helix to b-sheet and random-coil secondary structures was observedt hanks to FTIR spectroscopy.T his process has been reportedf or different proteins and radiationt ypes, for instance, bovine serum albumin (BSA) irradiatedb yN + ions [63] or protons, [64] although the underlying mechanism remains unclear.…”

Section: Irradiation By Ionizing Radiationmentioning

confidence: 99%

Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

et al. 2019

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In this review, recent progress in understanding the direct effects of radiation on the structure and stability of collagen, the most abundant protein in the human body, and other proteins is surveyed. Special emphasis is placed on the triple‐helical structure of collagen, as studied by means of collagen mimetic peptides. The emerging patterns are the dose dependence of radiation processes and their abundance, the crucial role of radicals in covalent‐bond formation (crosslinking) or cleavage, and the influence of the radiation energy and nature. Future research should allow fundamental questions, such as charge transfer and fragmentation dynamics triggered by ionization, to be answered, as well as developing applications such as protein‐based biomaterials, notably with properties controlled by irradiation.

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Irradiation effects on secondary structure of protein induced by keV ions

Cited by 14 publications

References 21 publications

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)

Nanobacteria Are Mineralo Fetuin Complexes

Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

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Irradiation effects on secondary structure of protein induced by keV ions

Cited by 14 publications

References 21 publications

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K2HPO4 + H2O)

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K2HPO4 + H2O)

Nanobacteria Are Mineralo Fetuin Complexes

Direct Radiation Effects on the Structure and Stability of Collagen and Other Proteins

Contact Info

Product

Resources

About

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)

Structural and Partitioning Studies of Bovine Serum Albumin in Mixture of (Poly(ethylene glycol) + K₂HPO₄ + H₂O)