- Folding disulfide-containing proteins faster with an aromatic thiol
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The traditional method for in vitro folding of disulfide-containing proteins is slow and involves a redox buffer of glutathione and glutathione disulfide. To increase the folding rate and to gain insight into the folding process, we replaced glutathione, an aliphatic thiol, with a commercially available aromatic thiol, 4-mercaptobenzeneacetate (1). Aromatic thiol 1 was selected due to its enhanced nucleophilicity and its enhanced leaving-group ability relative to glutathione at pH 7.7. To demonstrate the advantages of 1, the folding of reduced and scrambled RNase A at pH 7.0 and 7.7 in the presence of 1 and glutathione was investigated. For each set of folding conditions, the optimum concentration of each thiol was initially determined and then the folding rates in the presence of each thiol were measured concurrently. In all cases examined, the folding rate enhancement with the aromatic thiol was 5- 6-fold. Furthermore, under similar conditions folding rates were almost identical with either reduced or scrambled RNase A. In addition the 5-6-fold folding rate enhancement varied only slightly with pH, 7.0 vs 7.7.
- Gough, Jonathan D.,Williams Jr., Rhondye H.,Donofrio, Anthony E.,Lees, Watson J.
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- Templated DNA ligation with thiol chemistry
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We describe two DNA-templated ligation strategies: native chemical ligation (NCL), and thiol-disulfide exchange. Both systems result in successful ligation in the presence of a DNA template. The stability of the product from the NCL reaction relies on exogenous thiol, while the thiol-disulfide reaction proceeds in a catalyst-free manner. This journal is
- Li, Dadong,Wang, Xiaojian,Shi, Fubo,Sha, Ruojie,Seeman, Nadrian C.,Canary, James W.
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- METHOD FOR PATHOGENS, MICROORGANISMS, AND PARASITES INACTIVATION
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The invention provides a method for inactivation or reduction of pathogens, microorganisms or parasites in a sample, media, composition, utility, device, surface or organism by treatment with an alkylating compound of Structure I, followed by elimination or reduction of the residual compound with Structure I by treatment with a neutralizing agent, which eliminates or reduces the toxicity or other undesirable properties of the alkylating compound with Structure I. The neutralizing agent may be present in a treatment solution or be part of a solid-phase agent, and preferably acts by eliminating the alkylating properties of the compound of Structure I.
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Paragraph 0221-0224
(2020/02/16)
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- Visible-Light Emulsion Photopolymerization of Styrene
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The photopolymerization of styrene in emulsion is achieved in a conventional double-wall reactor equipped with a LED ribbon coiled around the external glass wall. Styrene mixed to acridine orange is added to the water phase containing sodium dodecyl sulfate, a water-soluble N-heterocyclic carbene–borane and disulfide, and irradiated. Highly stable latexes are obtained, with particles up to a diameter of 300 nm. The ability to reach such large particle sizes via a photochemical process in a dispersed medium is due to the use of visible light: the photons in the visible range are less scattered by larger objects and thus penetrate and initiate better the polymerizations. They are also greener and cheaper to produce via LEDs, and much safer than UVs. The method presented does not require any specific glassware; it works at lower temperature and delivers larger particles compared to thermal processes at similar solids contents and surfactant concentrations.
- Le Quéméner, Frédéric,Subervie, Daniel,Morlet-Savary, Fabrice,Lalevée, Jacques,Lansalot, Muriel,Bourgeat-Lami, Elodie,Lac?te, Emmanuel
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p. 957 - 961
(2018/01/01)
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- Enzymatic thiol Michael addition using laccases: Multiple C-S bond formation between p-hydroquinones and aromatic thiols
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Laccases create C-C, C-O or C-N bonds and have been investigated intensively as catalysts for green chemistry and white biotechnology. However, little is known about C-S bond formation in laccase-catalyzed reactions. We have used the laccases from Pycnopo
- Schlippert, Max,Mikolasch, Annett,Hahn, Veronika,Schauer, Frieder
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supporting information
p. 106 - 114
(2016/02/27)
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- Hexitol derivatives having vasodilative activity
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Disclosed is a hexitol derivative represented by the formula (I): STR1 wherein Q represents a formula selected from the group consisting of STR2 wherein a represents NH, O or S; each of b, c and d independently represents CH or N; each of R1, R2, R3 and R4 independently represents hydrogen, lower alkyl, trifluoromethyl, aryl, lower alkanoyloxy, amino, lower alkylamino, lower alkanoylamino, lower alkanoyl, aroyl, halogen, nitro, (CH2)m OR 7, (CH2)m SR7, (CH2)m CO2 R7 where R7 represents hydrogen or lower alkyl and m represents an integer of 0 to 3; each of R5 and R6 independently represents hydrogen or lower alkyl; U represents >N-- or STR3 W represents a single bond, --O-- or --S--; X represents STR4 wherein each of Y1 and Y2 independently represents hydrogen, lower alkyl, hydroxyl, lower alkanoyloxy, nitrile or phenyl; or Y1 and Y2 are combined together to form oxygen; each of Y3 and Y4 independently represents hydrogen or lower alkyl; and l is an integer of 0 to 6, and where l is an integer of 2 to 6, each STR5 may be the same or different; Z represents hydrogen or nitro; and, n is 2 or 3 or a pharmaceutically acceptable salt thereof. The compounds show prominent coronary vasodilative activities, and are useful in treating angina pectoris and myocardial infarction.
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