Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra.

No abstract is available for this paper.

• Publication year

  2009

• Venue

  International journal of peptide & protein research

• Publication date

  2009-01-12

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1111/J.1399-3011.1986.TB02761.XPMID 3949437
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Equilibrium and kinetic study of sodium- and potassium-induced conformational changes of apo-alpha-lactalbumin.

  1985cited by this paper
• Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin.

  1985cited by this paper
• Metal ion binding to the N and A conformers of bovine alpha-lactalbumin.

  1984cited by this paper
• Amino group environments and metal binding properties of carbon-13 reductively methylated bovine alpha-lactalbumin.

  1984cited by this paper
• Nuclear magnetic resonance studies on calmodulin: calcium-dependent spectral change of proteolytic fragments

  1984cited by this paper
• Thermodynamics of thermal unfolding of bovine apo-alpha-lactalbumin.

  1984cited by this paper
• Conformational changes induced by zinc and terbium binding to native bovine alpha-lactalbumin and calcium-free alpha-lactalbumin.

  1984cited by this paper
• High-affinity binding of Ca2+ to bovine alpha-lactalbumin in the absence and presence of EGTA.

  1984cited by this paper
• Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins.

  1984cited by this paper
• NMR studies of muscle proteins.

  1984cited by this paper
• Statistical thermodynamical treatment of protein unfolding.

  1983cited by this paper
• Interactions of Divalent Metal Ions with Bovine, Human, and Goat α-Lactalbumins

  1983cited by this paper
• Interactions of divalent metal ions with bovine, human, and goat alpha-lactalbumins.

  1983cited by this paper
• Metal ion binding to alpha-lactalbumin species.

  1982cited by this paper
• Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin.

  1981cited by this paper
• Role of the interaction between ionizable groups in the folding of bovine alpha-lactalbumin.

  1981cited by this paper
• Binding of calcium to lysozyme and its derivatives.

  1981cited by this paper
• Thermodynamics of alpha-lactalbumin unfolding.

  1981cited by this paper
• Nuclear magnetic resonance characterization of aromatic residues of alpha-lactalbumins. Laser photo chemically induced dynamic nuclear polarization nuclear magnetic resonance studies of surface exposure.

  1981cited by this paper
• Calcium binding to alpha-lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes.

  1981cited by this paper
• Role of the Interaction between Ionizable Groups in the Folding of Bovine α-Lactalbumin

  1981cited by this paper
• Thermodynamics of α-lactalbumin unfolding

  1981cited by this paper
• Stability of troponin C.

  1980cited by this paper
• Dependence of NMR lineshape analysis upon chemical rates and mechanisms: Implications for enzyme histidine titrations

  1980cited by this paper
• alpha-Lactalbumin: a calcium metalloprotein.

  1980cited by this paper
• α-Lactalbumin: A calcium metalloprotein

  1980cited by this paper
• Stability of proteins: small globular proteins.

  1979cited by this paper
• The aromatic residues of bovine pancreatic ribonuclease studied by 1H nuclear magnetic resonance.

  1979cited by this paper
• Thermodynamic investigations of proteins. IV. Calcium binding protein parvalbumin.

  1978cited by this paper
• Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism.

  1978cited by this paper
• Calorimetric study on the conformational transition of alpha-lactalbumin induced by guanidine hydrochloride.

  1977cited by this paper
• Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride.

  1976cited by this paper
• Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)

  1976cited by this paper
• Three-state denaturation of α-lactalbumin by guanidine hydrochloride

  1976cited by this paper
• Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C

  1976cited by this paper
• Proton-magnetic-resonance spectroscopic study of the histidine residues of bovine alpha-lactalbumin.

  1975cited by this paper
• Convolution difference 1H NMR spectra at 360 MHz of the basic pancreatic trypsin inhibitor

  1975cited by this paper
• Critical factors in the design of sensitive high resolution nuclear magnetic resonance spectrometers

  1975cited by this paper
• Lactose synthetase.

  1975cited by this paper
• Computation of structures of homologous proteins. Alpha-lactalbumin from lysozyme.

  1974cited by this paper
• A possible three-dimensional structure of bovine alpha-lactalbumin based on that of hen's egg-white lysozyme.

  1969cited by this paper
• 1349. Thermodynamics of ion association. Part XII. EGTA complexes with divalent metal ions

  1965cited by this paper
• Komplexone XXXVI. Reakinsenthalpie und ‐entropie bei der Bildung der Metallkomplexe der höheren EDTA‐Homologen

  1964cited by this paper

• Investigation of the Proteolytic Potential of Isolates of the Genus Lactobacillus Obtained from Homemade Bulgarian Cow, Sheep, Buffalo yoghurt and lactic acid products, for the Hydrolysis of Whey Proteins using Tris-Tricine-SDS Polyacrylic Amide Gel Electrophoresis

  2021cites this paper
• α-Lactalbumin, Amazing Calcium-Binding Protein

  2020cites this paper
• Control of α-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine.

  2018cites this paper
• Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding.

  2016cites this paper
• The effect of pH and temperature pre-treatments on the structure, surface characteristics and emulsifying properties of alpha-lactalbumin.

  2015cites this paper
• Macromolecular Crowding Induces Holo α-Lactalbumin Aggregation by Converting to Its Apo Form

  2014cites this paper
• Global and local indices for characterizing biomolecular flexibility and rigidity

  2013cites this paper
• Energetic domains analysis of bovine α-lactalbumin upon interaction with copper and dodecyl trimethylammonium bromide

  2010cites this paper
• Influence of zinc(II) binding on the structure of bovine alpha-lactalbumin.

  2009cites this paper
• Studies on cell-clearing activity in alpha-lactalbumin. Effects of calcium removal on activity and conformation.

  2009cites this paper
• The Human α-Lactalbumin Molten Globule: Comparison of Structural Preferences at pH 2 and pH 7

  2009cites this paper
• Energetics of solvent and ligand‐induced conformational changes in α‐lactalbumin

  2008cites this paper
• Repliement des protéines et formation de fibres amyloïdes. Le cas de l'alpha-lactalbumine

  2008cites this paper
• A false paradise - mixed blessings in the protein universe: the amyloid as a new challenge in drug development.

  2007cites this paper
• The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics.

  2006cites this paper
• Differential Scanning Calorimetry of a Metalloprotein under Controlled Metal–Ion Activity

  2006cites this paper
• 8 Protein-Protein Interactions in Food

  2006cites this paper
• A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine alpha-lactalbumin.

  2005cites this paper
• Effects of heat and of near-UV irradiation on goat alpha-lactalbumin.

  2005cites this paper
• Stability of HAMLET—A kinetically trapped α‐lactalbumin oleic acid complex

  2005cites this paper
• A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine α-lactalbumin

  2005cites this paper
• Thermodynamics of Mn2+-binding to goat α-lactalbumin

  2004cites this paper
• Tyrosine group behaviour in bovine α-lactalbumin as revealed by its Raman effect

  2004influential citation
• Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule, and unfolded states.

  2004cites this paper
• Characterisation of intermediate(s) in the folding pathway of porcine growth hormone / by Emma Jane Parkinson.

  2004cites this paper
• A Non-Native α-Helix Is Formed in the β-Sheet Region of the Molten Globule State of Canine Milk Lysozyme

  2004cites this paper
• A non-native alpha-helix is formed in the beta-sheet region of the molten globule state of canine milk lysozyme.

  2004cites this paper
• Ca(2+) and Na(+) binding to high affinity sites of calcium-containing proteins measured by capillary electrophoresis.

  2003cites this paper
• Structural Basis for Difference in Heat Capacity Increments for Ca2+ Binding to Two α-Lactalbumins

  2002cites this paper
• Detection and resolution of intermediate species in protein folding processes using fluorescence and circular dichroism spectroscopies and multivariate curve resolution.

  2002cites this paper
• Structural basis for difference in heat capacity increments for Ca(2+) binding to two alpha-lactalbumins.

  2002cites this paper
• Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.

  2001cites this paper
• Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme.

  2000cites this paper
• A calorimetric study of the influence of calcium on the stability of bovine alpha-lactalbumin.

  2000cites this paper
• Effects of soybean saponin on protease hydrolyses of beta-lactoglobulin and alpha-lactalbumin.

  2000cites this paper
• Effects of Soybean Saponin on Protease Hydrolyses of β-Lactoglobulin and α-Lactalbumin

  2000cites this paper
• Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule

  2000cites this paper
• A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin.

  2000cites this paper
• Effect of hydrostatic pressure on unfolding of α‐lactalbumin: Volumetric equivalence of the molten globule and unfolded state

  1999cites this paper
• Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine alpha-lactalbumin: the stabilizing role of the calcium ion.

  1999cites this paper
• Tertiary contacts in alpha-lactalbumin at pH 7 and pH 2: a molecular dynamics study.

  1998cites this paper
• Effect of natural ligands on the structural properties and conformational stability of proteins.

  1998cites this paper
• Production of correctly folded recombinant [13C, 15N]-enriched guinea pig [Val90]-alpha-lactalbumin.

  1997cites this paper
• Effects of organic solvents on protein structures: Observation of a structured helical core in hen egg‐white lysozyme in aqueous dimethylsulfoxide

  1997cites this paper
• Structures and functionalities of milk proteins.

  1996cites this paper
• Thermodynamic characterization of the partially unfolded state of Ca(2+)-loaded bovine alpha-lactalbumin: evidence that partial unfolding can precede Ca2+ release.

  1996cites this paper
• Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin.

  1996cites this paper
• Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature.

  1996cites this paper
• Molten-Globule State of Carbonic Anhydrase Binds to the Chaperone-like α-Crystallin*

  1996cites this paper
• Pb2+ and Hg2+ binding to alpha-lactalbumin.

  1996cites this paper
• Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach

  1996cites this paper
• Thermal unfolding of beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin. A thermodynamic approach.

  1996cites this paper
• Molten globule and protein folding.

  1995cites this paper
• Thermodynamic parameters for 3-state thermal denaturation of human and bovine α-lactalbumin

  1995cites this paper
• A three-state heat-denaturation of bovine α-lactalbumin

  1995cites this paper
• Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study.

  1994cites this paper
• Conformational comparison between alpha-lactalbumin and lysozyme.

  1994cites this paper
• Differential scanning calorimetry : a useful tool for studying protein denaturation

  1994cites this paper
• Conformational comparison between α-lactalbumin and lysozyme

  1994cites this paper
• Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin.

  1993cites this paper
• Characterization of the stable, acid‐induced, molten globule‐like state of staphylococcal nuclease

  1993cites this paper
• Effect of Sodium and Calcium Addition on Thermal Denaturation of Apo-α-Lactalbumin: a Differential Scanning Calorimetric Study

  1993cites this paper
• Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule.

  1993cites this paper
• Conformational aspects of the Cu2+ binding to alpha-lactalbumin. Characterization and stability of the Cu-bound state.

  1992cites this paper
• The effect of calcium on bovine α-lactalbumin conformational transitions by ultraviolet difference and fluorescence spectrophotometry

  1992cites this paper
• Thermodynamic analysis of the effect of calcium on bovine alpha-lactalbumin conformational stability

  1992cites this paper
• Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.

  1992cites this paper
• Absence of the thermal transition in apo-α-lactalbumin in the molten globule state

  1992cites this paper
• DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat.

  1992cites this paper
• Effect of metal ion binding on the secondary structure of bovine alpha-lactalbumin as examined by infrared spectroscopy.

  1991cites this paper
• A circular dichroic study of Cu(II) binding to bovine α-lactalbumin

  1991cites this paper
• Lysozyme and alpha-lactalbumin: structure, function, and interrelationships.

  1991cites this paper
• Protein and enzyme stability: structural, thermodynamic, and experimental aspects.

  1991cites this paper
• A circular dichroic study of Cu(II) binding to bovine alpha-lactalbumin.

  1991cites this paper
• Thermodynamics of Mn(2+)-binding to goat alpha-lactalbumin.

  1991cites this paper
• Analysis of calcium binding to alpha-lactalbumin using a fluorescent calcium indicator.

  1991cites this paper
• A structural study of calcium-binding equine lysozyme by two-dimensional 1H-NMR.

  1991cites this paper
• Analysis of calcium binding to α‐lactalbumin using a fluorescent calcium indicator

  1991cites this paper
• Effect of metal ion binding on the secondary structure of bovine alpha-lactalbumin as examined by infrared spectroscopy.

  1991cites this paper
• NMR studies of the structure and environment of the milk protein alpha-lactalbumin.

  1990cites this paper
• Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry.

  1990cites this paper
• Hydrogen exchange of the tryptophan residues in bovine, goat, guinea pig, and human alpha-lactalbumin.

  1989cites this paper
• Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin.

  1989cites this paper
• Metal-Ion Binding and the Molecular Conformational Properties of α Lactalbumi

  1989cites this paper
• The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

  1989cites this paper
• Contribution of disulfide bonds to stability of the folding intermediate of alpha-lactalbumin.

  1989cites this paper
• Metal-ion binding and the molecular conformational properties of alpha lactalbumin.

  1989cites this paper
• Proteins in whey: chemical, physical, and functional properties.

  1989cites this paper
• Calorimetric experiments of Mn2+-binding to α-lactalbumin

  1988cites this paper
• Characterization of the foaming properties of lysozymes and α-lactalbumins: a structural evaluation

  1988cites this paper
• Calorimetric experiments of Mn2+ -binding to alpha-lactalbumin.

  1988cites this paper
• Methionine-90-spin-labeled bovine alpha-lactalbumin: electron spin resonance and NMR distance measurements.

  1988cites this paper
• Hydrogen exchange of the tryptophan residues in bovine α‐lactalbumin studied by uv spectroscopy

  1988cites this paper
• Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength

  1988cites this paper
• Hydrogen exchange of the tryptophan residues in bovine alpha-lactalbumin studied by UV spectroscopy.

  1988cites this paper
• Protein folding: Hypotheses and experiments

  1987cites this paper
• Comparison of the binding of Na+ and Ca2+ to bovine alpha-lactalbumin.

  1987cites this paper
• Comparison of the binding of Na+ and Ca2+ to bovine α-lactalbumin

  1987cites this paper
• Tyrosine group behaviour in bovine alpha-lactalbumin as revealed by its Raman effect.

  1987cites this paper
• Binding strength of calcium ion to bovine alpha-lactalbumin.

  1986cites this paper