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Chinese Journal of Chemical Physics 2023年第5期36卷 517-525,I0001页

作者： Xinfei Li Xiaodong Chen Ning Chen Liming Liu Xiaoguo Zhou Shilin Liu Department of Chemical Physics University of Science and Technology of ChinaHefei 230026China

Nickel,an important transi-tion metal element,is one of the trace elements for hu-man body and has a crucial impact on life and *** evidences show the excess exposure to metal ions might be associated with neurological ***,we applied Raman spectroscopy to study the Ni(II)ion effect on kinetics of amyloid fibrillation of hen egg white lysozyme(HEWL)in thermal and acidic *** the well-known Raman indicators for protein tertiary and secondary structures,we monitored and analyzed the concentration effect of Ni(II)ions on the unfolding of tertiary structures and the transformation of sec-ondary *** experimental evidence validates the accelerator role of the metal ion in the ***,the additional analysis of the amide I band profile,combined with thioflavin-T fluorescence assays,clearly indicates the inhibitory effect of Ni(II)ions on the formation of amyloid fibrils with organizedβ-sheets ***,a more significant promotion influence is affirmed on the assembly into other aggregates with disordered *** present results provide rich information about the specific metal-mediated protein fibrillation.

关键词： Amyloid fibrillation protein denaturation Kinetics Nickel ion Lysozyme

Specific protein-urea interactions

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Magnetic Resonance Letters 2022年第3期2卷 131-138页

作者： Zhi Wei Wong Daiwen Yang Department of Biological Sciences National University of Singapore14 Science Drive 4Singapore117543Singapore

The mechanism of urea's action in protein denaturation remains largely *** provide an experimental basis for molecular dynamics(MD)simulations on urea-protein interactions,we investigated the effect of urea on human intestinal fatty acid binding protein(hIFABP)by nuclear magnetic resonance(NMR).Hydrogen-deuterium exchange(HDX)rates at2 M urea indicate that urea affects hIFABP in a residue-specific manner via direct urea-protein interactions and preferentially weakens hydrogen bonds between highly protected ***-specific effects of urea on NMR peak intensities and chemical shifts further support the presence of direct urea-protein ***(2D)water-rotating frame Overhauser enhancement(ROE)data shows one protein-bound water molecule in contact with Val66 and Trp82,one putative bound water molecule in interaction with Thr76 and E-F loop,and that urea at low concentrations cannot displace these protein-bound water *** urea-nuclear Overhauser effect(NOE)experiments using 15N-urea further show no tightly protein-bound urea *** results thus suggest specific,but weak or transient,urea-protein interactions,supporting the direct interaction model of urea denaturation.

关键词： protein denaturation protein-folding Fatty acid binding protein Hydrogen-deuterium exchange

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UBC32 Mediated Oxidative Tolerance in Arabidopsis

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Journal of Genetics and Genomics 2012年第8期39卷 415-417页

作者： Feng Cui Lijing Liu Qingliang Li Chengwei Yang Qi Xie State Key Laboratory of Plant Genomics National Center for Plant Gene Research Institute of Genetics and Developmental Biology Chinese Academy of Sciences Beijing 100101 China Guangdong Key Lab of Biotechnology for Plant Development College of Life Science South China Normal University Guangzhou 510631 China

Extreme environments such as salt stress often increase the reactive oxygen species （ROS） levels （Abogadallah, 2010; Miller et al., 2010）, which cause protein denaturation and damage （Kelsen et al., 2008）. In eukaryotic cells, the endo- plasmic reticulum （ER） lumen is highly oxidative environment, which help newly synthesized proteins form intermolecular or intramolecular disulfide bonds between their cysteine residues. However, the ROS must be regulated according to the folding load to protect the cell from the consequences of oxidative folding.

关键词： reactive oxygen species endoplasmic reticulum protein denaturation salt stress

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Preparation of Bovine Serum Albumin Microspheres by an Acetone-ethanol Heat denaturation Method

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Journal of Chinese Pharmaceutical Sciences 1997年第2期6卷 28-35页

作者：何琳陈国强路英杰陈金春清华大学生物科学与技术系

Stable sub 500 nm bovine serum albumin (BSA) microsphere suspensions were produced by controlled addition of acetone and ethanol to an aqueous solution of BSA, followed by stabilization process of the formed microspheres at an elevated temperature. Microspheres produced by this acetone ethanol heat denaturation method were stabilized at relatively low temperatures (70～75℃) over a short period of time (20 min). The acetone ethanol heat denaturation method, in comparison with the traditional oil/ water technique for preparation of albumin microspheres, which requires high temperature (over 100℃) and longer heating time (more than 30 min) for stabilization, offers a number of advantages. This report describes the influence of process conditions, such as ratios of acetone to ethanol to BSA aqueous solution, heating time and heating temperature, on microsphere formation and their stability. A loading efficiency of 40% rose bengal was achieved. Rose bengal release rates from these microspheres in phosphate buffered saline medium at 37 ℃ were dependent on microsphere stabilities and 25% to 60% of initial loading drug were released in 15 days.

关键词： Bovine serum albumin Microsphere manufacture protein denaturation Rose bengal Release study Microencapsulation

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Opinion: hazards faced by macromolecules when confined to thin aqueous films

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Biophysics Reports 2017年第Z1期3卷 1-7页

作者： Robert M.Glaeser Bong-Gyoon Han Lawrence Berkeley National Laboratory University of California

Samples prepared for single-particle electron cryo-microscopy(cryo-EM) necessarily have a very high surface-to-volume ratio during the short period of time between thinning and vitrification. During thi time, there is an obvious risk that macromolecules of interest may adsorb to the air–water interface with a preferred orientation, or that they may even become partially or fully unfolded at the interface In addition, adsorption of macromolecules to an air–water interface may occur even before thinning This paper addresses the question whether currently used methods of sample preparation might be improved if one could avoid such interfacial interactions. One possible way to do so might be to preemptively form a surfactant monolayer over the air–water interfaces, to serve as a structure-friendly slide and coverslip. An alternative is to immobilize particles of interest by binding them to some type o support film, which—to continue using the analogy—thus serves as a slide. In this case, the goal is no only to prevent the particles of interest from diffusing into contact with the air–water interface but also to increase the number of particles seen in each image. In this direction, it is natural to think o developing various types of affinity grids as structure-friendly alternatives to thin carbon films. Perhap ironically, if precautions are not taken against adsorption of particles to air–water interfaces, sacrificia monolayers of denatured protein may take the roles of slide, coverslip, or even both.

关键词： Sample preparation Cryo-EM Air–water interface protein denaturation