Collagen from Salted Jellyfish (Rhopilema esculentum): Structural Characterization, Emulsifying Properties and Wound Healing Potential [PDF]
GelsJellyfish collagen, a sustainable and biocompatible marine biomaterial, holds great potential in food and biomedical applications. This study explores the emulsification properties and therapeutic potential of pepsin-soluble collagen derived from salt ...
Bing Hu +7 more
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Investigation of DNA denaturation from generalized Morse potential
Materials and Devices, 2018 In this paper, we present a non-linear model for the study of DNA denaturation transition. To this end, we assume that the double-strands DNA interact via a realistic generalized Morse potential that reproduces well the features of the real ...
R. El Kinani, H. Kaidi, M. Benhamou
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A DSC study of zinc binding to bovine serum albumin (BSA) [PDF]
Journal of the Serbian Chemical Society, 2007 The thermal denaturation of bovine serum albumin (BSA) is a kinetically and thermodynamically controlled process. The effects of zinc binding to bovine serum albumin (BSA), followed by differential scanning calorimetry (DSC), were investigated in this ...
SANJA OSTOJIC +3 more
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Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics. [PDF]
PLoS ONE, 2011 Despite several careful experimental analyses, it is not yet clear whether protein cold-denaturation is just a "mirror image" of heat denaturation or whether it shows unique structural and energetic features. Here we report that, for a well-characterized
M Luisa Romero-Romero +3 more
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Irreversible denaturation of maltodextrin glucosidase studied by differential scanning calorimetry, circular dichroism, and turbidity measurements. [PDF]
PLoS ONE, 2014 Thermal denaturation of Escherichia coli maltodextrin glucosidase was studied by differential scanning calorimetry, circular dichroism (230 nm), and UV-absorption measurements (340 nm), which were respectively used to monitor heat absorption ...
Megha Goyal +2 more
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Foods, 2023 The kinetic properties and thermal characteristics of fresh pork meat proteins (Longissimus dorsi), as well as osmotically dehydrated meat proteins, were investigated using differential scanning calorimetry.
Sanja Ostojić +5 more
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DNA-binding function of c-Myb R2R3 around thermal denaturation temperature
Biophysics and Physicobiology, 2021 The minimum DNA-binding domain of the transcriptional factor c-Myb R2R3 remarkably fluctuates in the solution. In the present study, we evaluated the protein fluctuation of R2R3 C130I mutant, R2R3*, on its DNA-binding and folding thermodynamics.
Maki Kawasaki, Masayuki Oda
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The regulatory subunit of PKA-I remains partially structured and undergoes β-aggregation upon thermal denaturation. [PDF]
PLoS ONE, 2011 BackgroundThe regulatory subunit (R) of cAMP-dependent protein kinase (PKA) is a modular flexible protein that responds with large conformational changes to the binding of the effector cAMP.
Khanh K Dao +7 more
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Polar or apolar--the role of polarity for urea-induced protein denaturation. [PDF]
PLoS Computational Biology, 2008 Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood.
Martin C Stumpe, Helmut Grubmüller
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Molecules, 2022 The functional structure of proteins results from marginally stable folded conformations. Reversible unfolding, irreversible denaturation, and deterioration can be caused by chemical and physical agents due to changes in the physicochemical conditions of
Patrick Masson, Sofya Lushchekina
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