Results 21 to 30 of about 65,216 (256)

Papain denaturation is not a two‐state transition

open access: yesFEBS 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.
openaire   +2 more sources

Honey-Induced Protein Stabilization as Studied by Fluorescein Isothiocyanate Fluorescence

open access: yesThe 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
doaj   +1 more source

Coil–globule transition in the denatured state of a small protein [PDF]

open access: yesProceedings 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.
Eilon, Sherman, Gilad, Haran
openaire   +2 more sources

Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress

open access: yesGels, 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
doaj   +1 more source

Topological Origin of the Phase Transition in a Model of DNA Denaturation [PDF]

open access: yesPhysical Review Letters, 2004
8 pages, 1 figure, RevTex 4; v2: minor changes in the ...
Grinza, Paolo, Mossa, Alessandro
openaire   +3 more sources

Calorimetric and spectroscopic investigation of the unfolding of human apolipoprotein B.

open access: yesJournal 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
doaj   +1 more source

Free cysteine modulates the conformation of human C/EBP homologous protein. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat

open access: yesCzech Journal of Food Sciences, 2011
The cryoprotective effects of trehalose and maltose (w = 2-10%) on washed beef meat were investigated. Washed beef meat produced from fresh beef meat was frozen and stored for 360 days at -30°C.
Dragan Kovačević   +1 more
doaj   +1 more source

RNA Denaturation: Excluded Volume, Pseudoknots, and Transition Scenarios [PDF]

open access: yesPhysical Review Letters, 2003
4 pages 3 ...
BAIESI, MARCO   +2 more
openaire   +3 more sources

Calorimetric Study of Helix aspersa Maxima Hemocyanin Isoforms

open access: yesJournal 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
doaj   +1 more source

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