Journal ArticleDOI
Secondary structures of bovine serum albumin in anionic and cationic surfactant solutions
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TLDR
In this article, secondary structure changes of bovine serum albumin were examined in solutions of sodium decyl sulfate (SDeS), sodium dodecyl sulfates (SDS), decyltrimethylammonium bromide (DeTAB), dodecynthimethylmoniam bromides (DTAB) and hexadecyltrimylmonium Bromide(HTAB); the relative proportions of α-helix, β-structure, and random coil were estimated by simulating a mixed circular dichroismAbout:
This article is published in Journal of Colloid and Interface Science.The article was published on 1987-05-01. It has received 86 citations till now. The article focuses on the topics: Sodium dodecyl sulfate & Pulmonary surfactant.read more
Citations
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Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: A comparative study of the two and one tryptophan(s) of bovine and human albumins
TL;DR: Differences in the fluorescence behavior of the proteins are attributed to the fact that Trp-134 exists only in BSA, with the assumption thattrimethylammonium bromide behaves the same asTrp-214 of HSA, which appears to relate to the disruption of the helical structure in the SDS solution.
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Conformational change of bovine serum albumin by heat treatment.
TL;DR: The thermal denaturation of bovine serum albumin (BSA) was studied at pH 2.8 and 7.0 in the range of 2–65°C and the structural change was reversible in the temperature range below 45°C, but was partially reversible upon cooling to room temperature subsequent to heating at 65°C.
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Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130 °C and Protective Effect of Sodium Dodecyl Sulfate on the Change
TL;DR: This protective effect of SDS, characterized by the specific amphiphilic nature of this anionic surfactant, is considered to be attained by building cross-linking bridges between particular nonpolar residues and particular positively charged residues in the protein molecule.
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Protective effect of small amounts of sodium dodecyl sulfate on the helical structure of bovine serum albumin in thermal denaturation
TL;DR: In the presence of sodium dodecyl sulfate (SDS), the secondary structure of bovine serum albumin (BSA) was almost protected against thermal denaturation above 50 degrees C, where the structural change became irreversible.
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Ionic liquids induced structural changes of bovine serum albumin in aqueous media: a detailed physicochemical and spectroscopic study.
TL;DR: CD combined with the steady state fluorescence spectroscopy provided valuable insights into the unfolding of BSA as a consequence of IL binding as well as drawing out the mechanism of interaction between ILs and BSA in different IL concentration regimes.
References
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Computed circular dichroism spectra for the evaluation of protein conformation
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Estimation of globular protein secondary structure from circular dichroism.
S W Provencher,J Glöckner +1 more
TL;DR: In this article, a linear combination of the CD spectra (from 190 to 240 nm) of 16 proteins whose secondary structures are known from X-ray crystallography was used to characterize helix, beta sheet, beta turn, and remainder.
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Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.
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Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion.
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Circular dichroic analysis of protein conformation: inclusion of the beta-turns.
TL;DR: In this paper, the mean residue ellipticity, [theta], at any wavelength, lambda, of a protein in aqueous solution is expressed as ε = fH[theta]H infinity(1-k/n) + f beta[thet]beta + ft[thetea]t + fR[ theta]R with two constraints: 1 > or = fj > 0 and sigma fj = 1.