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2021 ◽  
Vol 89 ◽  
pp. 103102
Author(s):  
Johanne Nedergaard ◽  
Mark Schram Christensen ◽  
Mikkel Wallentin
Keyword(s):  

2021 ◽  
Author(s):  
Johanne Nedergaard ◽  
Mark Schram Christensen ◽  
Mikkel Wallentin

In this paper, we aimed to test whether we could predict sport type (badminton or running) and marathon proficiency from the valence, form, and content of the athletes’ self-reported inner speech. Additionally, we wanted to assess the difference between self-talk during high intensity and low intensity exercise. The present study corroborated existing research – we were able to predict both sport type in Study 1 and intensity level as well as marathon proficiency in Study 2 from questionnaire data using machine learning models. In Study 1, we found that badminton players engage more in worry and anxiety-control while runners are more prone to task disengagement. Interestingly, it seemed in Study 2 that the more participants engaged in condensed, positive, and repetitive self-talk when not pushing themselves, the slower their fastest marathons and half marathons were. We discuss potential explanations for these findings and make suggestions for future research.


2020 ◽  
Vol 90 (9) ◽  
pp. 1462
Author(s):  
С.В. Валуева ◽  
Т.Е. Суханова ◽  
М.Э. Вылегжанина ◽  
Т.К. Мелешко

The morphological, spectral and molecular conformational characteristics of amphiphilic molecular brushes with polyimide main chain and polymetacrylic acid side chains loaded with a second-generation photosensitizer Radachlorin® or nanoparticles of the biogenic element – selenium in the zero–valence form were studied using atomic force microscopy (AFM), UV-vis spectroscopy and dynamic/static light scattering. The influence of the side chains grafting density of amphiphilic molecular brushes and the hydrophobic preparation/agent loaded into them on the morphological, spectral and molecular conformational characteristics of synthesized binary nanosystems is shown.


Biochemistry ◽  
1999 ◽  
Vol 38 (23) ◽  
pp. 7565-7571 ◽  
Author(s):  
Borries Rost ◽  
Julia Behr ◽  
Petra Hellwig ◽  
Oliver-Matthias H. Richter ◽  
Bernd Ludwig ◽  
...  

1994 ◽  
Vol 300 (2) ◽  
pp. 469-475 ◽  
Author(s):  
N J Watmough ◽  
M R Cheesman ◽  
C Greenwood ◽  
A J Thomson

Oxidized cytochrome bo reacts rapidly with micromolar concentrations of H2O2 to form a single derivative. The electronic absorption spectrum of this compound differs from that of the oxidized form of the enzyme reported by this laboratory [Watmough, Cheesman, Gennis, Greenwood and Thomson (1993) FEBS Lett. 319, 151-154]. It is characterized by a Soret maximum at 411 nm, increased absorbance at 555 nm, and reduced intensity at 624 nm. The apparent dissociation constant for this process is of the order of 4 x 10(-6) M, and the bimolecular rate constant for the formation of the new compound is (1.25-1.7) x 10(3) M-1.s-1. Electronic absorption difference spectroscopy shows this product to be identical with the compound formed from the reaction of the mixed-valence form of the enzyme with dioxygen. Investigation of this compound by room-temperature magnetic c.d. spectroscopy shows haem o to be neither high-spin nor low-spin ferric, but to have a spectrum characteristic of an oxyferryl species. There is no evidence for oxidation of the porphyrin ring. Therefore the binuclear centre of this species must consist of an oxyferryl haem (S = 1) coupled to a Cu(II) ion (S = 1/2) to form a new paramagnetic centre. The reaction was also followed by X-band e.p.r. spectroscopy, and this showed the disappearance in parallel with the formation of the oxyferryl species, of the broad g = 3.7, signal which arises from the weakly coupled binuclear centre in the oxidized enzyme. Since no new e.p.r.-detectable paramagnetic species were observed, the Cu(II) ion is presumed to be coupled to another paramagnet, possibly an organic radical. There is no evidence in the electronic absorption spectrum to indicate further reaction of cytochrome bo with H2O2 to form a second species. We argue that the circumstances of formation of this oxyferryl species are the same as those for the P form of cytochrome c oxidase, a species often regarded as containing a bound peroxide ion. The implications of these observations for the reaction mechanism of haem-copper terminal oxidases are discussed.


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