The fitball as a multifunctional kinesitherapeutical instrument - specificity when choosing

Голямата гимнастическа топка „Fitball` (ГГТ) в последните години придоби популярност в световен мащаб. В наши дни освен като гимнастически и фитнес уред ГГТ се е наложила като ценен и широко прилаган метод в кинезитерапевтичната практика. Характеристиките на ГГТ изискват спазването на определени правила при избора й с оглед постигането на максимално лечебно въздействие и безопасност за пациента. Подборът на точния размер, цвят и разновидност са от съществено значение за прецизното изпълнение и ефективността на методиката. Познаването на технологичните характеристики и условията за съхранение и експлоатация на ГГТ гарантират безопасността при нейното използване.The big gymnastic ball `Fitball` has gained popularity worldwide in the last few years. Nowadays, except as gym and fitness equipment, Fitball has established itself as a valuable and widely used method in the kinesitherapeutic practice. The characteristics of Fitball require compliance with certain rules in selecting it to achieve maximum therapeutic effect and safety for the patient. The selection of the exact size, color and type are essential for precise execution and effectiveness of the methodology. Knowing the technological characteristics and conditions for storage and operation of Fitball ensure the safety of its use

The Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane Domains

The epidermal growth factor receptor (EGFR) is one of the most extensively studied receptor tyrosine kinases, as it is involved in a wide range of cellular processes and severe diseases. Recent works reveal that the single-helix transmembrane domains and cytoplasmic juxtamembrane regions play an important role in the receptor activation process. Here we present the results of our investigation of the spatial structure and mobility of the EGFR transmembrane domain and juxtamembrane regions in various membranelike environments, which shed light on the effects of the membrane physical properties and composition on the behavior of the juxtamembrane domain

Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration

International audienceIntrinsically disordered proteins (IDPs) underpin biological regulation and hence are highly desirable drug-development targets. NMR is normally the tool of choice for studying the conformational preferences of IDPs, but the association of regions with residual structure into partially collapsed states can lead to poor spectral quality. The bHLH-LZ domain of the oncoprotein Myc is an archetypal example of such behavior. To circumvent spectral limitations, we apply chemical denaturant titration (CDT)-NMR, which exploits the predictable manner in which chemical denaturants disrupt residual structure and the rapid exchange between conformers in IDP ensembles. The secondary structure propensities and tertiary interactions of Myc are determined for all bHLH-LZ residues, including those with poor NMR properties under native conditions. This reveals conformations that are not predictable using existing crystal structures. The CDT-NMR method also maps sites perturbed by the prototype Myc inhibitor, 10058-F4, to areas of residual structure