Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate

Mattice, Wayne L.; Riser, James M.; Clark, Donald S.

doi:10.1021/bi00664a020

Cited by 234 publications

(106 citation statements)

References 83 publications

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“…Analysis of these curves by the method of Provencher and Glockner (1981) showed that the a-helix and fl-sheet content of the two contrazymes were increased slightly in the presence of sodium dodecyl sulfate. Similar changes have been observed in several other globular proteins (Mattice et al 1976). There is, however, no marked difference between contrapsin and a-l-antitrypsin, indicating that the main chain structure of the two murine proteins are very similar in the presence of sodium dodecyl sulfate.…”

Section: Resultssupporting

confidence: 85%

Conformational differences between mouse contrapsin and .ALPHA.-1-antitrypsin as studied by ultraviolet absorption and circular dichroism spectroscopy.

Takahara

Shibata

Sinohara

1984

Tohoku J. Exp. Med.

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We have compared the conformation of mouse contrapsin, a novel trypsin inhibitor (Takahara, H. and Sinohara, H. (1982) J. biol. Chem., 257, 2438-2446, and a-l-antitrypsin by UV absorption and CD spectroscopy. The two mouse inhibitors share a similar secondary structure, i.e., 24-29% a-helix, 31% /-sheet, and 10-11% /l-turn. The corresponding values for human a-l-antitrypsin are 48, 25, and 9%, respectively. These results suggest that peptide backbone structures of the two mouse inhibitors resemble each other, but differ slightly from that of human a-l-antitrypsin.On the other hand, evidence is accumulated that the microenvironments of aromatic side chains are considerably different in mouse contrapsin and a-l-antitrypsin : (i) An unusual fine vibrational structure was seen in the UV absorption spectra of murine and human a-l-antitrypsins, but not in that of contrapsin. (ii) CD bands in contrapsin which may be assigned to phenylalanyl residues were several-fold greater in intensity than those in the two a-l-antitrypins.(iii) The above-mentioned bands in contrapsin were more susceptible to pH changes than those in a-l-antitrypsin.(iv) CD bands in contrapsin which may contain unresolved contributions from tyrosyl and tryptophanyl residues also markedly differed from those in the two a-l-antitrypsins. These differences were, however, largely diminished in the presence of 50 mM sodium dodecyl sulfate, suggesting that mouse contrapsin and a-l-antitrypsin have a similar structure in the presence of this perturbant. UV absorption ; CD spectra ; mouse contrapsin ; mouse a-l-antitrypsin a-1-Antitrypsin or a-1-protease inhibitor is a glycoprotein which is responsible for about 90% of the trypsin-inhibiting capacity of human serum, and which

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Section: Resultssupporting

confidence: 85%

Conformational differences between mouse contrapsin and .ALPHA.-1-antitrypsin as studied by ultraviolet absorption and circular dichroism spectroscopy.

Takahara

Shibata

Sinohara

1984

Tohoku J. Exp. Med.

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“…Residual structure (at room temperature) in SDS denatured states of proteins is not uncommon. Serum albumin [19] and a number of other proteins show different degrees of secondary structure, when exposed to high concentrations of ionic surfactants [11,16,[52][53][54][55][56].…”

Section: Discussionmentioning

confidence: 99%

“…This anionic compound, which is generally considered a potent denaturant [4], was investigated in many early works on bovine serum albumin (BSA) [5][6][7][8][9][10] and a number of other proteins [11][12][13][14][15][16][17]. This led to several general conclusions regarding the modes of interaction of SDS and proteins (for reviews see [18][19][20]).…”

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confidence: 99%

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Bagger

Hoffmann

Fuglsang

et al. 2007

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractThe interactions of sodium dodecyl sulfate (SDS) and two glyco-variants of the enzyme phytase from Peniophora lycii were investigated. One variant (Phy) was heavily glycosylated while the other (dgPhy) was enzymatically deglycosylated. Effects at 24°C of titrating SDS to Phy and dgPhy were studied by Isothermal Titration Calorimetry (ITC) and Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. Comparisons of results for the two variants were used to elucidate glycan-surfactant interrelationships.The CD spectra suggested that both the native and the SDS-denatured states of the two variants were mutually similar, and hence that the denaturation process was structurally equivalent for the two glyco-variants.The denatured state was far from fully unfolded and probably retained a substantial content of native-like structure. Furthermore, it was found that the glycans brought about only a small increase in the resistance towards SDS induced denaturation. The SDS concentration required to denature half of the protein molecules differed less than 1 mM for the two variants.The affinity for SDS of both variants was unusually low. The amount of bound SDS (w/w) at different stages of the binding isotherm was 3-10 times lower than that reported for the most previously investigated globular proteins. Analysis of the relative affinity of the glycan and peptide moieties suggested that the carbohydrates bind much less surfactant. At saturation, glycans adsorbed about half as much SDS (in g/g) as the peptide moiety of Phy and about five times less than average proteins.

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“…TFE appears to stabilize the secondary structure for which a peptide has a propensity to form (Zhong & Johnson, 1992). SDS has also been shown to induce secondary structure formation in some peptides (Bansal et al, 1990;Zhong & Johnson, 1992); in the case of proteins, the situation is much more complex (Mattice et al, 1976). In aqueous 30% TFE and 50 mM aqueous SDS, the far-UV CD spectra in both solutions revealed minima at 220 nm and 208 nm, which are characteristic of peptides or proteins possessing a high percentage of helical content (Fig.…”

Section: Urea-gradien T Gel Electrophoresismentioning

confidence: 97%

Effect of pH and denaturants on the folding and stability of murine interleukin‐6

et al. 1993

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The conformation and stability of a recombinant mouse interleukin-6 (mlL-6) has been investigated by analytical ultracentrifugation, fluorescence spectroscopy, urea-gradient gel electrophoresis, and near-and far-ultraviolet circular dichroism. On decreasing the pH from 8.0 to 4.0, the tryptophan fluorescence of mIL-6 was quenched 40%, the midpoint of the transition occurring at pH 6.9. The change in fluorescence quantum yield was not due to unfolding of the molecule because the conformation of mIL-6, as judged by both urea-gradient gel electrophoresis and CD spectroscopy, was stable over the pH range 2.0-10.0. Sedimentation equilibrium experiments indicated that mIL-6 was monomeric, with a molecular mass of 22,500 Da over the pH range used in these physicochemical studies. Quenching of tryptophan fluorescence (20%) also occurred in the presence of 6 M guanidine hydrochloride upon going from pH 7.4 to 4.0 suggesting that an amino acid residue vicinal in the primary structure to one or both of the two tryptophan residues, Trp-36 and Trp-160, may be partially involved in the quenching of endogenous fluorescence. In this regard, similar results were obtained for a 17-residue synthetic peptide, peptide H1, which corresponds to an N-terminal region of mIL-6 (residues Val-27-Lys-43). The pH-dependent acid quenching of endogenous tryptophan fluorescence of peptide H1 was 30% in the random coil conformation and 60% in the presence of a-helix-promoting solvents. Replacement of His-33 with Ala-33 in peptide HI alleviated a significant portion of the pH-dependent quenching of fluorescence suggesting that the interaction of the imidazole ring of His-33 with the indole ring of Trp-36 is a major determinant responsible for the quenching of the endogenous protein fluorescence of mIL-6. Keywords: circular dichroism; denaturation; fluorescence studies; interleukin-6; protein structure Interleukin-6 is a multifunctional cytokine that acts on a wide variety of tissues to elicit a broad spectrum of biological functions including terminal differentiation of B cells, growth and differentiation of T cells, and regulation of the acute-phase responses. IL-6 is also capable of inducing the differentiation of hematopoietic progenitor cells and megakaryocytes (for reviews see Kishimoto [1989], Van Snick [19901, and Gordon& Hoffman [1992]). Abbreviutions: IL-6, interleukin-6; m-, murine; h-, human; GdnHC1, guanidine hydrochloride; SDS, sodium dodecyl sulfate; MES, 2-(N-morpho1ino)ethane sulfonic acid; S, weight average sedimentation coefficient; [ B ] M~~, mean residue ellipticity; HEPES, N-2-hydroxyethylpiperazine-N1-2-ethane sulfonic acid; Tris, Tris(hydroxymethy1)aminomethane; CAPS, 3-(cyclohexylamino)-I-propane sulfonic acid; TFE, trifluoroethanol; GM-CSF, granulocyte-macrophage colony-stimulating factor.

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Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate

Cited by 234 publications

References 83 publications

Conformational differences between mouse contrapsin and .ALPHA.-1-antitrypsin as studied by ultraviolet absorption and circular dichroism spectroscopy.

Conformational differences between mouse contrapsin and .ALPHA.-1-antitrypsin as studied by ultraviolet absorption and circular dichroism spectroscopy.

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Effect of pH and denaturants on the folding and stability of murine interleukin‐6

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