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Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin
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title
Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin
(English)
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author
S. J. Yewdall
series ordinal
5
object named as
S J Yewdall
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author name string
S Brownlow
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1
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J H Morais Cabral
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2
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R Cooper
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3
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D R Flower
series ordinal
4
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I Polikarpov
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6
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A C North
series ordinal
7
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L Sawyer
series ordinal
8
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publication date
15 April 1997
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published in
Structure
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volume
5
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issue
4
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page(s)
481-95
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cites work
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
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Homology and structure-function correlations between alpha 1-acid glycoprotein and serum retinol-binding protein and its relatives
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Protein structure. One fold among many.
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The lipocalin protein family: structure and function
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Interaction of fatty acids with beta-lactoglobulin and albumin from ruminant milk
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Binding of long chain fatty acids to β-lactoglobulin
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Binding of p-nitrophenyl phosphate and other aromatic compounds by beta-lactoglobulin
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Occurrence of Different Beta-Lactoglobulins in Cow's Milk
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Location of sulfhydryl and disulfide groups in bovine .beta.-lactoglobulins and effects of urea
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Thermodenaturation of bovine -lactoglobulin. Kinetics and the introduction of -structure
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Crystal forms of β-lactoglobulin
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Structure of bovine β-lactoglobulin at 6Å resolution
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Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution
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PROCHECK: a program to check the stereochemical quality of protein structures
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Assessment of protein models with three-dimensional profiles
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Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution
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Crystallographic refinement of human serum retinol binding protein at 2A resolution
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Three-dimensional arrangement of conserved amino acid residues in a superfamily of specific ligand-binding proteins.
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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
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Hydrogen bonding in globular proteins
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Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution.
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The state of amino acid residues in β-lactoglobulin
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Exposure of Tyrosine Residues in Protein. Reaction of Cyanuric Fluoride with Ribonuclease, α-Lactalbumin, and β-Lactoglobulin*
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Tryptophan-19 of beta-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure
1 reference
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Expression and secretion of recombinant ovine beta-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis
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Sulphydryl groups and the N--R conformational change of beta-lactoglobulin
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Accessibility and mobility of lysine residues in beta-lactoglobulin
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The CCP4 suite: programs for protein crystallography
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Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
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Structure and sequence relationships in the lipocalins and related proteins
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Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC.
1 reference
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Spectroscopic characterization of beta-lactoglobulin-retinol complex
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Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
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Identifiers
DOI
10.1016/S0969-2126(97)00205-0
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PubMed ID
9115437
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ResearchGate publication ID
238310607
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