@article{baghurst_effect_nodate,
	title = {The {Effect} of {D},{Q} on the {Association} of {P}-{Lactogllobulin} {A}},
	abstract = {The association-dissociation equilibrium of the genetic variant fi-lactoglobulin A has been studied in an aqueous environment (acetate buffer, pH 4.65, I’/2 = 0.1) and one in which D,O replaced \&O (pD 4.65). Sedimentation velocity experiments (analyzed with respect to the area distribution of bimodal reaction boundaries and weight-average sedimentation coefficients) indicated that the extent of association was increased in the heavy water medium. The conclusion was supported by results obtained by Sephadex chromatography and by treatment of the MoffittYang parameter, ii{\textasciitilde},derived from optical rotatory dispersion studies, as a weight-average quantity. The latter method was alsoused to evaluate enthalpy changes associatedwith polymer formation in the two environments, the values being -64 and -69 kcal per mole in the Hz0 and DzO media, respectively. The results are compared with the stabilizing effect of DzO previously reported for other proteins and discussedin terms of increased interactions of both hydrogen bonding and hydrophobic types.},
	language = {en},
	author = {Baghurst, Peter A and Nichol, W and Sawyer, William H},
	keywords = {⛔ No DOI found},
	pages = {7},
}

{"_id":"gXhvJy48eHxWgX7w6","bibbaseid":"baghurst-nichol-sawyer-theeffectofdqontheassociationofplactogllobulina","author_short":["Baghurst, P. A","Nichol, W","Sawyer, W. H"],"bibdata":{"bibtype":"article","type":"article","title":"The Effect of D,Q on the Association of P-Lactogllobulin A","abstract":"The association-dissociation equilibrium of the genetic variant fi-lactoglobulin A has been studied in an aqueous environment (acetate buffer, pH 4.65, I’/2 = 0.1) and one in which D,O replaced &O (pD 4.65). Sedimentation velocity experiments (analyzed with respect to the area distribution of bimodal reaction boundaries and weight-average sedimentation coefficients) indicated that the extent of association was increased in the heavy water medium. The conclusion was supported by results obtained by Sephadex chromatography and by treatment of the MoffittYang parameter, ii~,derived from optical rotatory dispersion studies, as a weight-average quantity. The latter method was alsoused to evaluate enthalpy changes associatedwith polymer formation in the two environments, the values being -64 and -69 kcal per mole in the Hz0 and DzO media, respectively. The results are compared with the stabilizing effect of DzO previously reported for other proteins and discussedin terms of increased interactions of both hydrogen bonding and hydrophobic types.","language":"en","author":[{"propositions":[],"lastnames":["Baghurst"],"firstnames":["Peter","A"],"suffixes":[]},{"propositions":[],"lastnames":["Nichol"],"firstnames":["W"],"suffixes":[]},{"propositions":[],"lastnames":["Sawyer"],"firstnames":["William","H"],"suffixes":[]}],"keywords":"⛔ No DOI found","pages":"7","bibtex":"@article{baghurst_effect_nodate,\n\ttitle = {The {Effect} of {D},{Q} on the {Association} of {P}-{Lactogllobulin} {A}},\n\tabstract = {The association-dissociation equilibrium of the genetic variant fi-lactoglobulin A has been studied in an aqueous environment (acetate buffer, pH 4.65, I’/2 = 0.1) and one in which D,O replaced \\&O (pD 4.65). Sedimentation velocity experiments (analyzed with respect to the area distribution of bimodal reaction boundaries and weight-average sedimentation coefficients) indicated that the extent of association was increased in the heavy water medium. The conclusion was supported by results obtained by Sephadex chromatography and by treatment of the MoffittYang parameter, ii{\\textasciitilde},derived from optical rotatory dispersion studies, as a weight-average quantity. The latter method was alsoused to evaluate enthalpy changes associatedwith polymer formation in the two environments, the values being -64 and -69 kcal per mole in the Hz0 and DzO media, respectively. The results are compared with the stabilizing effect of DzO previously reported for other proteins and discussedin terms of increased interactions of both hydrogen bonding and hydrophobic types.},\n\tlanguage = {en},\n\tauthor = {Baghurst, Peter A and Nichol, W and Sawyer, William H},\n\tkeywords = {⛔ No DOI found},\n\tpages = {7},\n}\n\n","author_short":["Baghurst, P. A","Nichol, W","Sawyer, W. H"],"key":"baghurst_effect_nodate","id":"baghurst_effect_nodate","bibbaseid":"baghurst-nichol-sawyer-theeffectofdqontheassociationofplactogllobulina","role":"author","urls":{},"keyword":["⛔ No DOI found"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/eric.larG4","dataSources":["4i5C7S78DvJNsaHyg","5L2zM5wNE5CBYNuea"],"keywords":["⛔ no doi found"],"search_terms":["effect","association","lactogllobulin","baghurst","nichol","sawyer"],"title":"The Effect of D,Q on the Association of P-Lactogllobulin A","year":null}