Results 21 to 30 of about 131,881 (286)
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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Papain denaturation is not a two‐state transition
FEBS Letters, 1978 . Even proteins such as lysozyme [2] which has a cleft in the middle and parvalbumin [3] which consists of two distinct domains are denatured without stable intermediate states. This led to a tempting conclusion that all small globular proteins built of one poly- peptide chain represent a single cooperative system.
Tiktopulo, E.I., Privalov, P.L.
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Direct observation of large temperature fluctuations during DNA thermal denaturation [PDF]
, 2006 In this paper we report direct measurement of large low frequency temperature fluctuations in double stranded (ds) DNA when it undergoes thermal denaturation transition.
Chatterji, Dipankar +2 more
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Topological Origin of the Phase Transition in a Model of DNA Denaturation [PDF]
Physical Review Letters, 2004 8 pages, 1 figure, RevTex 4; v2: minor changes in the ...
Grinza, Paolo, Mossa, Alessandro
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Honey-Induced Protein Stabilization as Studied by Fluorescein Isothiocyanate Fluorescence
The Scientific World Journal, 2013 Protein stabilizing potential of honey was studied on a model protein, bovine serum albumin (BSA), using extrinsic fluorescence of fluorescein isothiocyanate (FITC) as the probe.
Yin How Wong +2 more
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Gels, 2022 Alpha-crystallin protein performs structural and chaperone functions in the lens and comprises alphaA and alphaB subunits at a molar ratio of 3:1. The highly complex alpha-crystallin structure challenges structural biologists because of its large dynamic
Ajamaluddin Malik +3 more
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Coil–globule transition in the denatured state of a small protein [PDF]
Proceedings of the National Academy of Sciences, 2006 Upon transfer from strongly denaturing to native conditions, proteins undergo a collapse that either precedes folding or occurs simultaneously with it. This collapse is similar to the well known coil–globule transition of polymers. Here we employ single-molecule fluorescence methods to fully characterize the equilibrium coil–globule ...
Eilon, Sherman, Gilad, Haran
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Free cysteine modulates the conformation of human C/EBP homologous protein. [PDF]
PLoS ONE, 2012 The C/EBP Homologous Protein (CHOP) is a nuclear protein that is integral to the unfolded protein response culminating from endoplasmic reticulum stress.
Vinay K Singh +5 more
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Calorimetric and spectroscopic investigation of the unfolding of human apolipoprotein B.
Journal of Lipid Research, 1990 The unfolding of human apolipoprotein B-100 in its native lipid environment, low density lipoprotein (LDL), and in a soluble, lipid-free complex with sodium deoxycholate (NaDC) has been examined using differential scanning calorimetry (DSC) and near UV ...
MT Walsh, D Atkinson
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Calorimetric Study of Helix aspersa Maxima Hemocyanin Isoforms
Journal of Analytical Methods in Chemistry, 2018 The thermal unfolding of hemocyanin isoforms, β-HaH and αD+N-HaH, isolated from the hemolymph of garden snails Helix aspersa maxima, was studied by means of differential scanning calorimetry (DSC). One transition, with an apparent transition temperature (
Svetla Todinova +2 more
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