Results 11 to 20 of about 65,216 (256)
Pepsinogen denaturation is not a two‐state transition [PDF]
FEBS Letters, 1981 1. introduction The knowledge of the mode of the denaturation reaction of proteins is important not only to under- stand their mechanism of folding, but also to obtain infomlation on their structural organization. From this point of view pepsinogen is one of the most inter- esting objects, since it is sufficiently large (M, 40 000) and its denaturation
Mateo, Pedro L., Privalov, Peter L.
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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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Disorder and denaturation transition in the generalized Poland–Scheraga model [PDF]
Annales Henri Lebesgue, 2020 We investigate the generalized Poland–Scheraga model, which is used in the bio-physical literature to model the DNA denaturation transition, in the case where the two strands are allowed to be non-complementary (and to have different lengths).
Quentin Berger +2 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 dynamics of the DNA denaturation transition [PDF]
EPL (Europhysics Letters), 2012 The dynamics of the DNA denaturation is studied using the Peyrard-Bishop-Dauxois model. The denaturation rate of double stranded polymers decreases exponentially as function of length below the denaturation temperature. Above Tc, the rate shows a minimum, but then increases as function of length.
van Erp, Titus S., Peyrard, Michel
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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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Order of the Phase Transition in Models of DNA Thermal Denaturation [PDF]
Physical Review Letters, 2000 We examine the behavior of a model which describes the melting of double-stranded DNA chains. The model, with displacement-dependent stiffness constants and a Morse on-site potential, is analyzed numerically; depending on the stiffness parameter, it is shown to have either (i) a second-order transition with "nu_perpendicular" = - beta = 1, "nu_parallel"
Theodorakopoulos, Nikos +2 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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Comment on “Why is the DNA Denaturation Transition First Order?” [PDF]
Physical Review Letters, 2003 In this comment we argue that while the conclusions in the original paper (Y. Kafri, D. Mukamel and L. Peliti, Phys. Rev. Lett. 85, 4988 (2000)) are correct for asymptotically long DNA chains, they do not apply to the chains used in typical experiments.
Hanke, Andreas, Metzler, Ralf
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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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