Journal ArticleDOI
‘New views’ on structure–function relationships in milk proteins
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TLDR
In this paper, it was shown that caseins share many of the same properties and may therefore exist naturally in a molten globule-like state with defined secondary structure and limited fluctuating tertiary structure, which lead to their propensity for polymerization.Abstract:
The molten globule state has been regarded as a major intermediate in protein folding. It is characterized by native-like secondary structure with a compact molecular size but little specific tertiary structure. α-lactalbumin under various denaturing conditions has been considered a paradigm of the classical molten globule state. It has been shown that caseins share many of the same properties and may therefore exist naturally in a molten globule-like state with defined secondary structure and limited fluctuating tertiary structure, which lead to their propensity for polymerization. The architectural concepts of tensegrity may be used to describe, in part, the structure of casein polymers.read more
Citations
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Journal ArticleDOI
Functional improvement of milk whey proteins induced by high hydrostatic pressure.
TL;DR: The mechanism underlying pressure-induced changes in β-lactoglobulin, α- lactabumin, and bovine serum albumin is explained, and related to functional properties such as gel-forming ability, emulsifying activity, or foaming capacity are explained.
Journal ArticleDOI
Adsorption Behavior of Acidic and Basic Proteins onto Citrate-Coated Au Surfaces Correlated to Their Native Fold, Stability, and pI
TL;DR: The adsorption of eight different proteins (alpha-lactalbumin, bovine serum albumin, hemoglobin, myoglobin, cytochrome c, alpha-casein, and lysozyme) onto a model anionic surface was performed and was found to be independent of global protein charge.
Journal ArticleDOI
Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy
Chockry Barbana,M.D. Pérez,Lourdes Sánchez,Michèle Dalgalarrondo,Jean-Marc Chobert,Thomas Haertlé,Miguel Calvo +6 more
TL;DR: In this article, the interaction of bovine holo- and apo- α-lactalbumin with fatty acids was studied using a partition equilibrium technique and fluorescence spectroscopy.
Journal ArticleDOI
Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study
TL;DR: Results of spectra analysis reveal differences in motional amplitudes of well-folded proteins, where β-sheet structures appear to be more rigid than a cluster of α-helices, and the disordered caseins display the largest conformational displacements.
Journal ArticleDOI
Fluorescent carbon dots from milk by microwave cooking
TL;DR: In this article, the formation of nanometre-sized, highly-fluorescent, nitrogen-doped carbon dots from milk by microwave cooking was reported, and the distribution of carbon dots in cells was confirmed by two-photon excited fluorescence intensity imaging and fluorescence lifetime imaging.
References
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Journal ArticleDOI
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
Journal ArticleDOI
Estimation of globular protein secondary structure from circular dichroism.
S W Provencher,J Glöckner +1 more
TL;DR: In this article, a linear combination of the CD spectra (from 190 to 240 nm) of 16 proteins whose secondary structures are known from X-ray crystallography was used to characterize helix, beta sheet, beta turn, and remainder.
Journal ArticleDOI
Are there pathways for protein folding
TL;DR: A pathway of folding means that there exist a well- defined sequence of events which follow one another so as to carry the protein from the unfolded random coil to a uniquely folded metastable state.
Journal ArticleDOI
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.
Book ChapterDOI
Molten globule and protein folding.
TL;DR: It is predicted and confirmed experimentally that the molten globule state can exist in a living cell and plays an important role in a number of physiological processes.