Sandbox Reserved 779: Difference between revisions

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[[Image:Beta_lac_2Q2M.png|thumb|right|320px|Bovine Beta-Lactoglobulin Native_2Q2M]]

===Relevant background ===

class of protein :Belongs to the calycin superfamily. Lipocalin family.

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== Structure of β-LG ==

At physiological conditions, bovine b-lactoglobulin forms a dimer, with each monomer consisting of 162 amino acid residues and characterized by a molecular mass of 18,350.1 Below pH 3, the dimer dissociates into monomers which preserve their native conformation.~~2±4~~ Genetically, b-lactoglobulin may exist as one of several variants, among which the variants A and B are the most abundant.1 The A and B variants of the protein differ from each other by amino acid residues at positions Asp64 (Gly64 in variant B) and Val118 (Ala118 in variant B). These differences in primary structure render the two variants slightly different with respect to isoelectric point, solubility, self-association properties, as well as pressure and temperature stability.~~5±7~~ However, the structural characteristics of the A and B variants of bovine b-lactoglobulin are virtually indistinguishable.8 In its native state, b-lactoglobulin is a predominantly b-sheet protein containing nine b-strands and three a-helices.~~8±10~~ The core of the protein is formed by a ~~¯attened~~ b-barrel (a calyx) composed of eight antiparallel b-strands (A to H). <ref>PMID:11734004</ref>

At physiological conditions, bovine b-lactoglobulin forms a dimer, with each monomer consisting of 162 amino acid residues and characterized by a molecular mass of 18,350. Below pH 3, the dimer dissociates into monomers which preserve their native conformation. Genetically, b-lactoglobulin may exist as one of several variants, among which the variants A and B are the most abundant. The A and B variants of the protein differ from each other by amino acid residues at positions Asp64 (Gly64 in variant B) and Val118 (Ala118 in variant B). These differences in primary structure render the two variants slightly different with respect to isoelectric point, solubility, self-association properties, as well as pressure and temperature stability. However, the structural characteristics of the A and B variants of bovine b-lactoglobulin are virtually indistinguishable. In its native state, b-lactoglobulin is a predominantly b-sheet protein containing nine b-strands and three a-helices. The core of the protein is formed by a flattened b-barrel (a calyx) composed of eight antiparallel b-strands (A to H).<ref>PMID:11734004</ref>

βLG consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol

Sandbox Reserved 779: Difference between revisions

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@@ Line 35: / Line 35: @@
 [[Image:Beta_lac_2Q2M.png|thumb|right|320px|Bovine Beta-Lactoglobulin Native_2Q2M]]
 ===Relevant background ===
 class of protein :Belongs to the calycin superfamily. Lipocalin family.
@@ Line 52: / Line 53: @@
 == Structure of β-LG ==
-At physiological conditions, bovine b-lactoglobulin forms a dimer, with each monomer consisting of 162 amino acid residues and characterized by a molecular mass of 18,350.1 Below pH 3, the dimer dissociates into monomers which preserve their native conformation.2±4 Genetically, b-lactoglobulin may exist as one of several variants, among which the variants A and B are the most abundant.1 The A and B variants of the protein differ from each other by amino acid residues at positions Asp64 (Gly64 in variant B) and Val118 (Ala118 in variant B). These differences in primary structure render the two variants slightly different with respect to isoelectric point, solubility, self-association properties, as well as pressure and temperature stability.5±7 However, the structural characteristics of the A and B variants of bovine b-lactoglobulin are virtually indistinguishable.8 In its native state, b-lactoglobulin is a predominantly b-sheet protein containing nine b-strands and three a-helices.8±10 The core of the protein is formed by a ¯attened b-barrel (a calyx) composed of eight antiparallel b-strands (A to H). <ref>PMID:11734004</ref>
+At physiological conditions, bovine b-lactoglobulin forms a dimer, with each monomer consisting of 162 amino acid residues and characterized by a molecular mass of 18,350. Below pH 3, the dimer dissociates into monomers which preserve their native conformation. Genetically, b-lactoglobulin may exist as one of several variants, among which the variants A and B are the most abundant. The A and B variants of the protein differ from each other by amino acid residues at positions Asp64 (Gly64 in variant B) and Val118 (Ala118 in variant B). These differences in primary structure render the two variants slightly different with respect to isoelectric point, solubility, self-association properties, as well as pressure and temperature stability. However, the structural characteristics of the A and B variants of bovine b-lactoglobulin are virtually indistinguishable. In its native state, b-lactoglobulin is a predominantly b-sheet protein containing nine b-strands and three a-helices. The core of the protein is formed by a flattened b-barrel (a calyx) composed of eight antiparallel b-strands (A to H).<ref>PMID:11734004</ref>
 βLG consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol