@article{MTMT:2972616,
	title = {How membrane proteins work giving autonomous traverse pathways?},
	url = {https://m2.mtmt.hu/api/publication/2972616},
	author = {Kardos, Julianna and Héja, László},
	doi = {10.1007/s11224-015-0601-0},
	journal-iso = {STRUCT CHEM},
	journal = {STRUCTURAL CHEMISTRY},
	volume = {26},
	unique-id = {2972616},
	issn = {1040-0400},
	abstract = {Enormous progress in computational chemistry shifted experiments toward predictive approaches. Such a paradigm shift applies to all branches of chemistry, especially to structural chemistry. To help the transfer of new knowledge in drug design practice, we reconsider a few vibrant topics of protein dynamics engaged in making predictions based on the timing of the events that are simulated. However, a complete explanation of the "dynamic evidence" also requires a reference to the time window allowing a prediction of the endpoint. Pioneering achievements disclosing the structure of large membrane proteins and their assemblies enabled the prediction of traverse pathways shaping membrane protein functions - essentially the efficacy of membrane proteins. Invoking significant advances made in characterizing the solute and ion symport of specific proteins through molecular dynamic simulations, early formation of a new type of solute-ion structure has been exposed as a prerequisite of Na+ symporter function. We demonstrate that the computational chemistry is one of the most appropriate models to study traverse pathways, and we also clarify the importance of the art of fast experimental techniques. © 2015 Springer Science+Business Media New York.},
	keywords = {TRANSPORTERS; Membrane Proteins; Traverse pathways; Sodium and chloride symport; Scaling dynamics; Concept review},
	year = {2015},
	eissn = {1572-9001},
	pages = {1405-1410}
}