The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein

dc.contributor.author	Papiz, M	en
dc.contributor.author	Sawyer, L	en
dc.contributor.author	Eliopoulos, E	en
dc.contributor.author	North, A	en
dc.contributor.author	Findlay, J	en
dc.contributor.author	Sivaprasadarao, R	en
dc.contributor.author	Jones, T	en
dc.contributor.author	Newcomer, M	en
dc.contributor.author	Kraulis, P	en
dc.date.accessioned	2014-06-06T06:41:31Z
dc.date.available	2014-06-06T06:41:31Z
dc.date.issued	1986	en
dc.identifier.uri	http://dx.doi.org/10.1038/324383a0	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/130
dc.subject	Binding Site	en
dc.subject	Model Building	en
dc.subject	Protein Folding	en
dc.subject	Retinol Binding Protein	en
dc.title	The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein	en
heal.type	journalArticle	en
heal.identifier.primary	10.1038/324383a0	en
heal.publicationDate	1986	en
heal.abstract	Since its first isolation1, bovine beta-lactoglobulin (BLG) has been an enigma: although it is abundant in the whey fraction of milk, its function is still not clear. The results of the many physicochemical studies on the protein need a structural interpretation. We report here the structure of the orthorhombic crystal form of cow BLG at pH 7.6, at a resolution	en
heal.journalName	Nature	en
dc.identifier.doi	10.1038/324383a0	en