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Relevant bibliographies by topics / Lysozyme; Trifluoroethanol; Guanidinium chloride

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Dissertations / Theses

Academic literature on the topic 'Lysozyme; Trifluoroethanol; Guanidinium chloride'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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Journal articles on the topic "Lysozyme; Trifluoroethanol; Guanidinium chloride"

1

Sasahara, Kenji, and Katsutoshi Nitta. "Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution." Protein Science 8, no. 7 (1999): 1469–74. http://dx.doi.org/10.1110/ps.8.7.1469.

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2

Duan, Haiyan, Xiandong Zeng, Biyu Tang, Xiaotao Liu, Guohua Lan, Wanzhi Wei, and Shenglian Luo. "Cooperative Effect of Guanidinium Chloride and Urea on Lysozyme Refolding." Analytical Letters 42, no. 16 (October 30, 2009): 2625–36. http://dx.doi.org/10.1080/00032710903243596.

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3

Field, J. M., A. S. Tatham, and P. R. Shewry. "The structure of a high-Mr subunit of durum-wheat (Triticum durum) gluten." Biochemical Journal 247, no. 1 (October 1, 1987): 215–21. http://dx.doi.org/10.1042/bj2470215.

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A high-Mr subunit was prepared from durum wheat (Triticum durum). Viscometric analysis showed that the molecule is rod-shaped, with molecular dimensions of about 50 nm x 1.75 nm (500 A x 17.5 A) in 0.05 M-acetic acid/0.01 M-glycine and 49 nm x 1.79 nm (490 A x 17.9 A) in aq. 50% (v/v) propan-1-ol (+/- 0.01 M-glycine) at 30 degrees C. C.d. spectroscopy in the same solvents indicated the presence of beta-turns, but little alpha-helix [7% in 50% (v/v) propan-1-ol] and no beta-sheet. However, when dissolved in trifluoroethanol the protein contains about 30% alpha-helix, and viscometric analysis gives dimensions of about 62 nm x 1.53 nm (620 A x 15.3 A). It is proposed, on the basis of these studies and previously published structural prediction, that the repetitive central domain of the high-Mr subunit forms a loose spiral based on repetitive beta-turns, whereas the shorter non-repetitive N- and C-terminal domains are alpha-helical in trifluoroethanol, but random coil in other solvents. The Mr of the high-Mr subunit determined from the intrinsic viscosity in 6.0 M-guanidinium chloride was 65,000, compared with 84,000 determined in 5.0 M-guanidinium thiocyanate. The latter value is consistent with the Mr values for related proteins whose complete amino acid sequences are known, and it was concluded that the protein is incompletely denatured in the former solvent. This was confirmed by c.d. spectroscopy in increasing concentrations (1-6 M) of guanidinium chloride.

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4

Ahmad, F., S. Yadav, and S. Taneja. "Determining stability of proteins from guanidinium chloride transition curves." Biochemical Journal 287, no. 2 (October 15, 1992): 481–85. http://dx.doi.org/10.1042/bj2870481.

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The guanidinium chloride (GdmCl) denaturation of RNAase A, lysozyme and metmyoglobin was investigated at several pH values by using absorbance measurements at 287, 300 and 409 nm respectively. From these measurements the free-energy change on denaturation, delta Gapp., was calculated, assuming a two-state mechanism, and values of delta Gapp. at zero concentration of the denaturant were measured. For each protein all delta Gapp. values were adjusted to pH 7.00 by using the appropriate relationship between delta Gapp. and pH. Dependence of the adjusted delta Gapp. value on GdmCl concentration increases for metmyoglobin and decreases for the other two proteins as the denaturant concentration decreases. It has been shown that these are expected results if the presence of the acid-denatured state during the GdmCl denaturation of proteins is considered.

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5

Kotik, Michael, Sheena E. Radford, and Christopher M. Dobson. "Comparison of the Refolding Hen Lysozyme from Dimethyl Sulfoxide and Guanidinium Chloride." Biochemistry 34, no. 5 (February 1995): 1714–24. http://dx.doi.org/10.1021/bi00005a028.

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6

Lyster, Richard L. J. "Effect of calcium on the stability of mares' milk lysozyme." Journal of Dairy Research 59, no. 3 (August 1992): 331–38. http://dx.doi.org/10.1017/s0022029900030600.

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SummaryThe three aspartic acid residues that form part of the Ca-binding site of mares' milk lysozyme have apparent pK values of 4·9, 4·3 and 4·1. The fluorescence of tryptophan has been used to compare the denaturation of mares' milk lysozyme by guanidinium chloride at various concentrations of Ca with that of hens' egg-white lysozyme (EC 3.2.1.17) and α-lactalbumin. Fluorescence revealed an intermediate stage in the denaturation of mares' milk lysozyme. The Ca-free form of mares' milk lysozyme is slightly more stable than that of α-lactalbumin, but its interaction with Ca is similar to that of α-lactalbumin, since only the native state binds Ca. Three-state models of denaturation can usefully be displayed on a ternary diagram.

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7

Dong, X. Y., J. H. Shi, and Y. Sun. "Cooperative Effect of Artificial Chaperones and Guanidinium Chloride on Lysozyme Renaturation at High Concentrations." Biotechnology Progress 18, no. 3 (June 7, 2002): 663–65. http://dx.doi.org/10.1021/bp0200191.

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8

Biswas, Biswajit, Aswathy N. Muttathukattil, Govardhan Reddy, and Prashant Chandra Singh. "Contrasting Effects of Guanidinium Chloride and Urea on the Activity and Unfolding of Lysozyme." ACS Omega 3, no. 10 (October 25, 2018): 14119–26. http://dx.doi.org/10.1021/acsomega.8b01911.

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9

Liu, Wei, Troy Cellmer, David Keerl, John M. Prausnitz, and Harvey W. Blanch. "Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements." Biotechnology and Bioengineering 90, no. 4 (2005): 482–90. http://dx.doi.org/10.1002/bit.20442.

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10

Chitra, Rajappa, and Paul E. Smith. "Molecular Association in Solution: A Kirkwood−Buff Analysis of Sodium Chloride, Ammonium Sulfate, Guanidinium Chloride, Urea, and 2,2,2-Trifluoroethanol in Water." Journal of Physical Chemistry B 106, no. 6 (February 2002): 1491–500. http://dx.doi.org/10.1021/jp011462h.

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More sources

Dissertations / Theses on the topic "Lysozyme; Trifluoroethanol; Guanidinium chloride"

1

Lu, Hui. "Studies of protein folding and unfolding using NMR and optical methods." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337421.

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2

Waldmann, Lars. "Effect of L-arginine and guanidinium chloride (GdmCl) on the unfolding and refolding of hen egg-white lysozyme (HEWL)." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975602772.

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3

Waldmann, Lars [Verfasser]. "Effect of L-arginine and guanidinium chloride (GdmCl) on the unfolding and refolding of hen egg-white lysozyme (HEWL) / von Lars Waldmann." 2005. http://d-nb.info/975602772/34.

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