scholarly journals The Dynamics of Hydrated Proteins Are the Same as Those of Highly Asymmetric Mixtures of Two Glass-Formers

ACS Omega ◽  
2020 ◽  
Author(s):  
Simone Capaccioli ◽  
Lirong Zheng ◽  
Apostolos Kyritsis ◽  
Alessandro Paciaroni ◽  
Michael Vogel ◽  
...  
Keyword(s):  
2008 ◽  
Vol 112 (32) ◽  
pp. 10071-10075 ◽  
Author(s):  
Stephen Bone

2005 ◽  
Vol 61 (a1) ◽  
pp. c116-c116
Author(s):  
J. C. Spence ◽  
B. Doak ◽  
U. Weierstall ◽  
K. Schmidt ◽  
P. Fromme ◽  
...  
Keyword(s):  

2013 ◽  
Vol 19 (No. 1) ◽  
pp. 19-23 ◽  
Author(s):  
L. Trojáková ◽  
Z. Réblová ◽  
Z. Pokorný

The storage of lipid foods is mostly affected by the oxidation of lipid fraction. Dry foods are particularly sensitive because lipids are not protected by hydrated proteins against oxidation. A method suitable for testing dry foods was studied in model mixtures of rapeseed oil with albumin or cellulose. Oxipres apparatus was used, where the course of oxidation is monitored by changes of oxygen pressure. The end of induction period was more evident than in bulk oils as the contact of lipids with oxygen is better. The induction period was longer in mixtures of edible oil with albumin than in mixtures with cellulose. The induction period moderately decreased with increasing oxygen pressure, while the effect of sample weight was nearly negligible. The induction period length was a semilogarithmic function of reaction temperature. Variation coefficients and differences between the duplicates showed good reproducibility; they were lower in mixtures with albumin than in mixtures with cellulose, but both were of the same order as the respective values in bulk oils. At 120°C and 0.5 MPa oxygen, the induction periods could be usually measured within a working day.


1991 ◽  
Vol 46 (1-2) ◽  
pp. 141-145 ◽  
Author(s):  
P PISSIS ◽  
A ANAGNOSTOPOULOUKONSTA

2003 ◽  
Vol 790 ◽  
Author(s):  
Jean-Pierre Korb ◽  
Robert G. Bryant

ABSTRACTWe present the frequency dependence of the proton spin-lattice relaxation rate 1/T1 in variously hydrated proteins. We present also the case of proteins confined in heavily hydrated gels where the rotation has been immobilized. The relaxation efficiency increases according to a power law at low frequencies. The temperature dependence of the protein protons T1 demonstrates that relaxation results from a direct spin-phonon process instead of a Raman process at temperatures above 273K. We propose a theory that accounts for experiments and depends on the dynamical distribution of states, the localization of the disturbances along and transverse to the peptide chains, and the spatial distribution of hydrogen in the structure. In hydrated and confined proteins, the motions of the backbone that dominate the relaxation process are transverse rather than along the peptide chain. We show that the protein structure adjusts to hydration from the lyophilized state to the fully hydrated state in small increment steps.


2012 ◽  
Vol 137 (16) ◽  
pp. 165101 ◽  
Author(s):  
Daniel R. Martin ◽  
Dmitry V. Matyushov

2011 ◽  
Vol 115 (19) ◽  
pp. 6222-6226 ◽  
Author(s):  
S. Khodadadi ◽  
J. E. Curtis ◽  
A. P. Sokolov

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