Effect of temperature on the interaction of cisplatin with the model protein hen egg white lysozyme

2016 ◽  
Vol 21 (4) ◽  
pp. 433-442 ◽  
Author(s):  
Giarita Ferraro ◽  
Andrea Pica ◽  
Irene Russo Krauss ◽  
Francesca Pane ◽  
Angela Amoresano ◽  
...  
Keyword(s):  
Egg White ◽  
Effect Of Temperature ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Model Protein ◽  
Hen Egg White ◽  
Hen Egg

Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

2015 ◽  
Vol 44 (22) ◽  
pp. 10392-10398 ◽  
Author(s):  
Daniela Marasco ◽  
Luigi Messori ◽  
Tiziano Marzo ◽  
Antonello Merlino
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Model Protein ◽  
Hen Egg White ◽  
Hen Egg

The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin.

Role of the osmolyte taurine on the folding of a model protein, hen egg white lysozyme, under a crowding condition

Amino Acids ◽  
2015 ◽  
Vol 47 (5) ◽  
pp. 909-915 ◽  
Author(s):  
Yoshito Abe ◽  
Takatoshi Ohkuri ◽  
Sachiko Yoshitomi ◽  
Shigeru Murakami ◽  
Tadashi Ueda
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Model Protein ◽  
Hen Egg White ◽  
Hen Egg

scholarly journals Probing temperature- and solvent-dependent protein dynamics using terahertz time-domain spectroscopy

2013 ◽  
Vol 47 (1) ◽  
pp. 146-153 ◽  
Author(s):  
Katarzyna M. Tych ◽  
Christopher D. Wood ◽  
Andrew D. Burnett ◽  
Arwen R. Pearson ◽  
A. Giles Davies ◽  
...  
Keyword(s):  
Single Crystal ◽  
Time Domain ◽  
Egg White ◽  
Effect Of Temperature ◽  
Hen Egg White Lysozyme ◽  
Terahertz Time Domain Spectroscopy ◽  
Time Domain Spectroscopy ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

The effect of temperature on the terahertz-frequency-range material properties of lyophilized and single-crystal hen egg-white lysozyme has been measured using terahertz time-domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg-white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature-dependent absorption coefficient is studied, and it is demonstrated that terahertz time-domain spectroscopy is capable of resolving the true glass transition temperature of single-crystal hen egg-white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

The inhibitory role of clioquinol in the fibrillation of hen egg white lysozyme

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Inhibitory Role ◽  
Hen Egg White ◽  
Hen Egg
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