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1.
Front Psychol ; 13: 1104143, 2022.
Artículo en Inglés | MEDLINE | ID: mdl-36698612

RESUMEN

Introduction: Athlete burnout has many potential negative effects on athletes' sporting performance and careers. Maintaining and promoting the coach-athlete relationship to meet athletes' basic psychological needs is one way to reduce burnout. Existing studies of the correlation between coach-athlete relationships and athlete burnout have mainly focused on the coaches' leadership style, with little attention given to relationship-maintenance strategies and the mechanism of athlete burnout from the athletes' perspective. Methods: Using an online survey of 256 adolescent athletes, we explore the relationship between relationship-maintenance strategies and athlete burnout, including the potential mediating effects of the coach-athlete relationship and basic psychological needs satisfaction. Results: (1) Athletes' relationship-maintenance strategies negatively predicted athlete burnout. (2) Besides the direct effect, we found evidence to support three mediation paths: (a) the coach-athlete relationship, (b) basic psychological needs satisfaction, and (c) both as serial mediators. Discussion: These findings enhance understanding of the mechanism of athlete burnout, demonstrating the influence of factors beyond the coach's role. The study also provides a theoretical basis for practical intervention by coaches, athletes, and sports organizations to reduce athlete burnout by focusing on athletes' perspectives.

2.
Front Psychol ; 11: 822, 2020.
Artículo en Inglés | MEDLINE | ID: mdl-32499737

RESUMEN

Sport psychology research has long sought to uncover the determinants of the optimal psychological state for peak performance. Persistent inquiries in this work include whether there is a set of ideal psychological and emotional factors that are required to achieve optimal performance and, if there are, what are they and how are they related to optimal performance. To answer these questions, the current study aimed to identify potential profiles of personality and emotional traits based on a sample of professional Taekwondo athletes from China. In addition, the study also aimed to examine the utility of the profiles in predicting successful athlete performance. Using multidimensional scaling (MDS) profile analysis, two latent profiles of personality and emotional traits were identified that indicate four subtypes of athletes. Regression analyses were conducted to examine how the identified profiles were associated with performance success. The results seemed to suggest that Taekwondo athletes with more performance success were more likely to have a profile of positive personality and emotional traits, while athletes with less performance success were likely to have somewhat elevated levels of self-control, extraversion, and aggression. Knowledge of athletes' personality profiles will help sport psychologists develop suitable interventions to enhance athletes' performance success. In concluding, the results are discussed in the context of athlete psychosocial development. The study added further evidence about the association between psychological and emotional factors and successful Taekwondo athletes.

3.
Nanotechnology ; 31(16): 165708, 2020 Apr 17.
Artículo en Inglés | MEDLINE | ID: mdl-31899912

RESUMEN

Fe-N-C catalyst obtained by high temperature pyrolysis is one of the most promising electrocatalysts for non-precious metal oxygen reduction reaction (ORR). However, up to now, the lesser density of active sites results in a substantial performance gap between the Fe-N-C materials and the conventional Pt/C ORR catalysts. Herein, an N-doped mesoporous carbon is employed as the support for the dispersion of poly-m-phenylenediamine. With high specific surface areas of 1526 m2 g-1, the as-prepared Fe-N-C materials show the half-wave potential of 0.89 V and 0.79 V in 0.1 M KOH and 0.5 M H2SO4, respectively. Notably, the superior methanol tolerance, as well as excellent stability, makes our Fe-N-C materials as competitive candidates for oxygen electrochemical catalysis.

4.
Sci Adv ; 5(4): eaau8164, 2019 04.
Artículo en Inglés | MEDLINE | ID: mdl-30989110

RESUMEN

NSF (N-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane fusion, to form a 20S complex, which disassembles the SNARE complex for reuse. We report the cryo-EM structures of the α-SNAP-SNARE subcomplex and the NSF-D1D2 domain in the 20S complex at 3.9- and 3.7-Å resolutions, respectively. Combined with the biochemical and electrophysiological analyses, we find that α-SNAPs use R116 through electrostatic interactions and L197 through hydrophobic interactions to apply force mainly on two positions of the VAMP protein to execute disassembly process. Furthermore, we define the interaction between the amino terminus of the SNARE helical bundle and the pore loop of the NSF-D1 domain and demonstrate its essential role as a potential anchor for SNARE complex disassembly. Our studies provide a rotation model of α-SNAP-mediated disassembly of the SNARE complex.


Asunto(s)
Fenómenos Mecánicos , Complejos Multiproteicos/química , Proteínas SNARE/química , Aminoácidos , Sitios de Unión , Modelos Moleculares , Complejos Multiproteicos/metabolismo , Complejos Multiproteicos/ultraestructura , Unión Proteica , Conformación Proteica , Dominios y Motivos de Interacción de Proteínas , Proteínas SNARE/metabolismo , Proteínas Solubles de Unión al Factor Sensible a la N-Etilmaleimida/química , Proteínas Solubles de Unión al Factor Sensible a la N-Etilmaleimida/metabolismo , Relación Estructura-Actividad
5.
Nat Commun ; 8: 16064, 2017 07 17.
Artículo en Inglés | MEDLINE | ID: mdl-28714467

RESUMEN

The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is essential for the machinery function by using the energy from ATP hydrolysis to disassemble the ESCRT-III polymer into individual proteins. Here, we report the structures of the ATP-bound Vps4E233Q hexamer and its complex with the cofactor Vta1 (vps twenty associated 1) at resolutions of 3.9 and 4.2 Å, respectively, determined by electron cryo-microscopy. Six Vps4E233Q subunits in both assemblies exhibit a spiral-shaped ring-like arrangement. Locating at the periphery of the hexameric ring, Vta1 dimer bridges two adjacent Vps4 subunits by two different interaction modes to promote the formation of the active Vps4 hexamer during ESCRT-III filament disassembly. The structural findings, together with the structure-guided biochemical and single-molecule analyses, provide important insights into the process of the ESCRT-III polymer disassembly by Vps4.


Asunto(s)
Adenosina Trifosfatasas/ultraestructura , Complejos de Clasificación Endosomal Requeridos para el Transporte/ultraestructura , Complejos Multiproteicos/ultraestructura , Proteínas de Saccharomyces cerevisiae/ultraestructura , Adenosina Trifosfatasas/metabolismo , Adenosina Trifosfato/metabolismo , Microscopía por Crioelectrón , Complejos de Clasificación Endosomal Requeridos para el Transporte/metabolismo , Escherichia coli , Complejos Multiproteicos/metabolismo , Saccharomyces cerevisiae , Proteínas de Saccharomyces cerevisiae/metabolismo , Imagen Individual de Molécula , Relación Estructura-Actividad
7.
J Biol Chem ; 282(44): 32256-63, 2007 Nov 02.
Artículo en Inglés | MEDLINE | ID: mdl-17785454

RESUMEN

Exchange proteins directly activated by cAMP (Epac) play important roles in mediating the effects of cAMP through the activation of downstream small GTPases, Rap. To delineate the mechanism of Epac activation, we probed the conformation and structural dynamics of Epac using amide hydrogen/deuterium exchange and structural modeling. Our studies show that cAMP induces significant conformational changes that lead to a spatial rearrangement of the regulatory components of Epac and allows the exposure of the catalytic core for effector binding without imposing significant conformational change on the catalytic core. Homology modeling and comparative structural analyses of the cAMP binding domains of Epac and cAMP-dependent protein kinase (PKA) lead to a model of Epac activation, in which Epac and PKA activation by cAMP employs the same underlying principle, although the detailed structural and conformational changes associated with Epac and PKA activation are significantly different.


Asunto(s)
Medición de Intercambio de Deuterio , Factores de Intercambio de Guanina Nucleótido/química , Espectrometría de Masas/métodos , Secuencia de Aminoácidos , AMP Cíclico/metabolismo , Proteínas Quinasas Dependientes de AMP Cíclico/química , Proteínas Quinasas Dependientes de AMP Cíclico/metabolismo , Factores de Intercambio de Guanina Nucleótido/metabolismo , Modelos Moleculares , Datos de Secuencia Molecular , Conformación Proteica , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo
8.
Biochemistry ; 45(51): 15318-26, 2006 Dec 26.
Artículo en Inglés | MEDLINE | ID: mdl-17176054

RESUMEN

Exchange proteins directly activated by cAMP (Epac) make up a family of cAMP binding domain-containing proteins that play important roles in mediating the effects of cAMP through the activation of downstream small GTPases, Ras-proximate proteins. To delineate the mechanism of Epac activation, we probed the conformation and structural dynamics of Epac using amide hydrogen-deuterium (H-D) exchange coupled with Fourier transform infrared spectroscopy (FT-IR) and structural modeling. Our studies show that unlike that of cAMP-dependent protein kinase (PKA), the classic intracellular cAMP receptor, binding of cAMP to Epac does not induce significant changes in overall secondary structure and structural dynamics, as measured by FT-IR and the rate of H-D exchange, respectively. These results suggest that Epac activation does not involve significant changes in the amount of exposed surface areas as in the case of PKA activation, and conformational changes induced by cAMP in Epac are most likely confined to small local regions. Homology modeling and comparative structural analyses of the CBDs of Epac and PKA lead us to propose a model of Epac activation. On the basis of our model, Epac activation by cAMP employs the same underlying structural principal utilized by PKA, although the detailed structural and conformational changes associated with Epac and PKA activation are significantly different. In addition, we predict that during Epac activation the first beta-strand of the switchboard switches its conformation to a alpha-helix, which folds back to the beta-barrel core of the CBD and interacts directly with cAMP to form the base of the cAMP-binding pocket.


Asunto(s)
Factores de Intercambio de Guanina Nucleótido/química , Factores de Intercambio de Guanina Nucleótido/metabolismo , Modelos Químicos , Modelos Moleculares , Secuencia de Aminoácidos , Proteína de Unión a Elemento de Respuesta al AMP Cíclico/química , Proteína de Unión a Elemento de Respuesta al AMP Cíclico/metabolismo , Medición de Intercambio de Deuterio , Humanos , Datos de Secuencia Molecular , Espectroscopía Infrarroja por Transformada de Fourier
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