Solution structure and dynamics of bovine β‐lactoglobulin A

Kuwata, Kazuo; Hoshino, Minoru; Forge, Vincent; Era, Seiichi; Batt, Carl A.; Goto, Yuji

doi:10.1110/ps.8.11.2541

Cited by 158 publications

(120 citation statements)

References 28 publications

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“…␤-Lactoglobulin contains one free sulfhydryl (Cys121) and two disulfide bonds (Cys66 -Cys160 and Cys106 -Cys119) [17]. It is a good model to demonstrate our strategy.…”

Section: Counting Both Free Sulfhydryls and Disulfide Bondsmentioning

confidence: 99%

Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag

Guo

Chen

Yang

et al. 2008

J. Am. Soc. Mass Spectrom.

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Organic mercurial compounds are the most specific and sensitive reagents for reaction with the sulfhydryl groups (OSHs) in peptides and proteins because of the strong mercury-sulfur affinity. Using the monofunctional organic mercury ion RHg ϩ as a mass spectrometry (MS)-tag has the advantages of reacting with one sulfhydryl group, offering definite mass shift, and especially stable and characteristic nonradioactive isotopic distribution. Mass spectrometric analysis of derivatized sulfhydryls in peptides/proteins is thus an alternative for precisely counting the number of sulfhydryl groups and disulfide bonds (OSOSO). Here the tags used include monomethylmercury chloride, monoethylmercury chloride, and 4-(hydroxymercuri) benzoic acid. The feasibility of this strategy is demonstrated using HPLC/ESI-MS to count OSHs and OSOSO in model peptides/proteins, i.e., glutathione, phytochelatins, lysozyme and ␤-lactoglobulin, which contain increasing OSHs and various OSOSO linkages. (J Am

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“…␤-Lactoglobulin contains one free sulfhydryl (Cys121) and two disulfide bonds (Cys66 -Cys160 and Cys106 -Cys119) [17]. It is a good model to demonstrate our strategy.…”

Section: Counting Both Free Sulfhydryls and Disulfide Bondsmentioning

confidence: 99%

Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag

Guo

Chen

Yang

et al. 2008

J. Am. Soc. Mass Spectrom.

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“…α-Domain consists of four α-helices, while domain β contains two β-sheets (Chrysina et al 2000). The secondary structure of bovine serum albumin does not include β-folded sheets and 68% of its secondary structure is composed of α-helices (Curry et al 1998;Kuwata et al 1999). MercadePrieto et al (2007) have calculated that the contents of the various structures in unheated β-lactoglobulin at pH 7.5 was 32.6% of β-sheet, 16.8% of α-helix, 20% of the reversed structures, and 27% were disordered.…”

mentioning

confidence: 99%

Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature

Tomczyńska‐Mleko¹,

Kamysz²,

Sikorska³

et al. 2014

Czech J. Food Sci.

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Tomczyńska-Mleko M., Kamysz E., Sikorska E., Puchalski C., Mleko S., Ozimek L., Kowaluk G., Gustaw W., Wesołowska-Trojanowska M. (2014): Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature. Czech J. Food Sci., 32: 82-89.The secondary structure of proteins in unheated and heated whey protein isolate dispersions and the surface tension of the solutions were investigated at different pH. Heating protein solutions at 80°C results in an increase of unordered structure. Nevertheless, the difference between the contents of unordered structure in the unheated and heated samples increases with increasing pH of the solution. At low protein concentrations the surface tension decreased with increasing protein concentration to about 5 mg/ml. For the heated solution, a similar trend was observed in the decrease in the surface tension with increasing concentrations of protein. In both cases, the curves depicting the surface tension as a function of protein concentration could be fitted to the exponential function with a negative exponent, but with the heated solutions lower values of surface tension were observed. Studies on the surface tension of whey protein isolate solutions prove that the unfolding of whey proteins, revealed by changes in the secondary structure, causes a decrease in the surface tension.

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“…2,3 However, the monomers retain their tertiary structures at acidic pH. Both crystal [4][5][6][7][8][9] and solution 10,11 structures of BLG show that the monomer contains nine b-strands (strands A-I), an ahelix, and three short 3 10 helices. Eight of the bstrands (A-H) form an up-and-down b-barrel, and the two I-strands form an intermolecular b-sheet containing four intermolecular hydrogen bonds.…”

mentioning

confidence: 99%

Structure and stability of Gyuba, a β‐lactoglobulin chimera

Ohtomo¹,

Konuma²,

Utsunoiya³

et al. 2011

Protein Science

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b-lactoglobulin (LG) contains nine b-strands (strands A-I) and one a-helix. Strands A-H form a b-barrel. At neutral pH, equine LG (ELG) is monomeric, whereas bovine LG (BLG) is dimeric, and the I-strands of its two subunits form an intermolecular b-sheet. We previously constructed a chimeric ELG in which the sequence of the I-strand was replaced with that of BLG. This chimera did not dimerize. For this study, we constructed the new chimera we call Gyuba (which means cow and horse in Japanese). The amino acid sequence of Gyuba includes the sequences of the BLG secondary structures and those of the ELG loops. The crystal structure of Gyuba is very similar to that of BLG and indicates that Gyuba dimerizes via the intermolecular b-sheet formed by the two I-strands. Thus, the entire arrangement of the secondary structural elements is important for LG dimer formation.

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Solution structure and dynamics of bovine β‐lactoglobulin A

Cited by 158 publications

References 28 publications

Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag

Counting sulfhydryls and disulfide bonds in peptides and proteins using mercurial ions as an MS-tag

Changes of secondary structure and surface tension of whey protein isolate dispersions upon pH and temperature

Structure and stability of Gyuba, a β‐lactoglobulin chimera

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