02985naa a2200301 a 450000100080000000500110000800800410001902400640006010000150012424501940013926000090033352019720034265000160231465000320233065300170236265300250237965300390240465300220244365300180246565300330248365300220251670000160253870000210255470000180257570000170259370000160261077300570262621691302025-08-25       2025    bl uuuu     u00u1 u    #d7 ahttp://dx.doi.org/10.2174/01246818732917662407240551362DOI1 aMAZONI, I.  aComprehensive analysis of the distinct nano environments characteristics containing the different secondary structure elementsbalpha-helices, beta-sheets, and turns.h[electronic resource]  c2025  aThis work is the third part of our initiative to fully describe the internal protein nano environments (NEs) for the three existing types of secondary structure elements (SSE). In our previous work, the NE of both the α-helix and the β-sheet were analyzed. The focus of this and previous research is improving our understanding of the SSEs: α-helices, β-sheets and turns, within protein structures. We found that the structural similarities between turns and α-helices are very high and turns may be considered as the “incomplete” initiation of α-helices. The knowledge we were able to compile during this work might be essential for predicting a tertiary structure of proteins, with higher precision and subsequently being in a more favourable position with regard to designing drugs for certain protein structure/function related diseases. Considering that the formation of secondary structure elements is a crucial step in the general folding of protein 3D structure, an important contribution of this work is augmenting the efficiency of estimating if modelled structures, for example, are predicting SSEs in full agreement to necessary/required/sufficient values of respective SSEs nanoenvironment descriptors. During exactly that modelling phase, preceding the more precise final 3D protein structure construction, our Dictionary of Most Relevant Nanoenvironment Descriptors is able to answer some fundamental questions regarding SSE correctness with regard to nanoenvironment characteristics found to be generally required. Expanding this vision, our current work is part of an effort by our laboratory to create a “dictionary of internal protein nanoenvironments” - DIPN. The ten most studied internal protein nanoenvironments are described in DIPN in physicochemical and structural terms, and this knowledge is now available to be used to aid drug design - probably the most important area of application for the results we are presenting here.  aAmino acids  aProtein secondary structure  aAminoácidos  aBanco de dados STING  aElementos de estrutura secundária  aNano environments  aNanoambientes  aSecondary structure elements  aSTING´s database1 aSALIM, J. A1 aMORAES, F. R. de1 aCORREA, J. L.1 aBORRO, L. C.1 aNESHICH, G.  tCurrent Nanomedicinegv. 15, n. 3, p. 267-285, 2025.