Kinetics of the self-aggregation and film formation of poly-L-proline at high temperatures explored by circular dichroism spectroscopy

Biopolymers ◽  
2009 ◽  
Vol 93 (5) ◽  
pp. 451-457 ◽  
Author(s):  
Lonna Tooke ◽  
Laura Duitch ◽  
Thomas J. Measey ◽  
Reinhard Schweitzer-Stenner
2021 ◽  
Vol 6 (8) ◽  
pp. 1735-1740
Author(s):  
Sora Lee ◽  
Soo Hyun Kim ◽  
You‐Young Jo ◽  
Wan‐Taek Ju ◽  
Hyun‐Bok Kim ◽  
...  

1998 ◽  
Vol 283 (1) ◽  
pp. 265-277 ◽  
Author(s):  
Mineyuki Mizuguchi ◽  
Munehito Arai ◽  
Yue Ke ◽  
Katsutoshi Nitta ◽  
Kunihiro Kuwajima

1998 ◽  
Vol 76 (6) ◽  
pp. 806-810 ◽  
Author(s):  
Teresa B Freedman ◽  
Diane L Hausch ◽  
Steven J Cianciosi ◽  
John E Baldwin

Vibrational circular dichoism spectra recorded for (2S,3S)-1-13C-1,2,3-d3-cyclopropane and for mixtures of it and the three related stereoisomers prepared through gas-phase thermal stereomutation reactions at 407°C lead to the rate constant for racemization: kα = (4k1 + 4k12) = (3.12 ± 0.04) x 10-5 s-1. This and the rate constant measured for geometrical equilibration between the two chiral and the two achiral stereoisomers of 1-13C-1,2,3-d3-cyclopropane, ki = (8k1 + 4k12) = (4.63 ± 0.20) x 10-5 s-1, give two equations in two unknowns, and allow one to solve for one-center (k1) and two-center (k12) epimerization rate constants for cyclopropane stereomutations. They are nearly equal, a clear indication of closely competitive reaction pathways.Key words: cyclopropane stereomutations, thermal epimerizations, chirality through deuterium and carbon-13 labeling, vibrational circular dichroism.


Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 998
Author(s):  
Laetitia Théron ◽  
Aline Bonifacie ◽  
Jérémy Delabre ◽  
Thierry Sayd ◽  
Laurent Aubry ◽  
...  

Food processing affects the structure and chemical state of proteins. In particular, protein oxidation occurs and may impair protein properties. These chemical reactions initiated during processing can develop during digestion. Indeed, the physicochemical conditions of the stomach (oxygen pressure, low pH) favor oxidation. In that respect, digestive proteases may be affected as well. Yet, very little is known about the link between endogenous oxidation of digestive enzymes, their potential denaturation, and, therefore, food protein digestibility. Thus, the objective of this study is to understand how oxidative chemical processes will impact the pepsin secondary structure and its hydrolytic activity. The folding and unfolding kinetics of pepsin under oxidative conditions was determined using Synchrotron Radiation Circular Dichroism. SRCD gave us the possibility to monitor the rapid kinetics of protein folding and unfolding in real-time, giving highly resolved spectral data. The proteolytic activity of control and oxidized pepsin was investigated by MALDI-TOF mass spectrometry on a meat protein model, the creatine kinase. MALDI-TOF MS allowed a rapid evaluation of the proteolytic activity through peptide fingerprint. This study opens up new perspectives by shifting the digestion paradigm taking into account the gastric digestive enzyme and its substrate.


2021 ◽  
Author(s):  
Kun Won Lee ◽  
Ahmed H. E. Hassan ◽  
Youngdo Jeong ◽  
Seolmin Yoon ◽  
Seung-Hwan Kim ◽  
...  

Enantioseparation and assignment of absolute configuration of methoxetamine (MXE) enantiopure stereoisomers; a promising novel antidepressant for management of treatment-resistant depression.


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