Digital Marketing Tools for Managing the Development of Park and Recreation Complexes

Digital marketing tools are actively used in managing the development of park and recreation complexes to familiarize the population with the objects of natural heritage. This article aims to empirically evaluate digital marketing tools for popularizing the park and recreational complexes. The methodology was based on the concept of ecosystem value of park and recreation complexes as a natural heritage site. These methods included: identifying and selecting websites with information about park and recreation complexes in Slovakia and Ukraine. structural analysis of the main channels of online details about natural parks. Assessing the current state of online identity of the studied sites from the perspective of Internet users. The results indicate that to manage the development of park and recreational complexes developed their driven official websites in the Internet space, on which sections structure the information with the allocation of data on tourism and recreational potential. The article identifies additional digital marketing tools for managing the development of park and recreation complexes, particularly social networks and tourist websites. There is a sufficient amount of information about tourist recreation sites within these natural parks and tourist routes. Among the main problems of the websites: the information on the websites is entirely textual, there is a lack of sufficient data on social networks, despite the created official pages, there is no video content, which was more attracted tourists and visitors, allowing a visual assessment of the tourist potential; there is a problem of many communication channels to present the natural heritage of the countries. The research proves that the website is the primary and most common digital marketing tool for natural heritage, structuring information about tourism potential and recreation

13C and15N NMR Study of the Hydration Response of T4 Lysozyme and αB-Crystallin Internal Dynamics

The response to hydration of the internal protein dynamics was studied by the means of solid state NMR relaxation and magic angle spinning exchange techniques. Two proteins, lysozyme from bacteriophage T4 and human aB-crystallin were used as exemplars. The relaxation rates R1 and R1? of 13C and 15N nuclei were measured as a function of a hydration level of the proteins in the range 0-0.6 g of water/g of protein. Both proteins were totally 15N-enriched with natural 13C abundance. The relaxation rates were measured for different spectral bands (peaks) that enabled the characterization of the dynamics separately for the backbone, side chains, and CH3 and NH3+ groups. The data obtained allowed a comparative analysis of the hydration response of the protein dynamics in different frequency ranges and different sites in the protein for two different proteins and two magnetic nuclei. The most important result is a demonstration of a qualitatively different response to hydration of the internal dynamics in different frequency ranges. The amplitude of the fast (nanosecond time scale) motion gradually increases with increasing hydration, whereas that of the slow (microsecond time scale) motion increases only until the hydration level 0.2-0.3 g of water/g of protein and then shows almost no hydration dependence. The reason for such a difference is discussed in terms of the different physical natures of these two dynamic processes. Backbone and side chain nuclei show the same features of the response of dynamics with hydration despite the fact that the backbone motional amplitudes are much smaller than those of side chains. Although T4 lysozyme and aB-crystallin possess rather different structural and biochemical properties, both proteins show qualitatively very similar hydration responses. In addition to the internal motions, exchange NMR data enabled the identification of one more type of motion in the millisecond to second time scale that appears only at high hydration levels. This motion was attributed to the restricted librations of the protein as a whole