caa a22 4500 445820780 CHVBK 20180317145243.0 cr unu---uuuuu 170323e20111001xx s 000 0 eng 10.1007/s00239-011-9465-0 doi (NATIONALLICENCE)springer-10.1007/s00239-011-9465-0 Amphiphilic α-Helical Potential: A Putative Folding Motif Adding Few Constraints to Protein Evolution [Elektronische Daten] [S. Lee, William Parker] Evidence from a number of studies indicates that protein folding is dictated not only by factors stabilizing the native state, but also by potentially independent factors that create folding pathways. How natural selection might cope simultaneously with two independent factors was addressed in this study within the framework of the "Lim-model” of protein folding, which postulates that the early stages of folding of all globular proteins, regardless of their native structure, are directed at least in part by potential to form amphiphilic α-helices. For this purpose, the amphiphilic α-helical potential in randomly ordered amino acid sequences and the conservation in phylogeny of amphiphilic α-helical potential within various proteins were assessed. These analyses revealed that amphiphilic α-helical potential is a common occurrence in random sequences, and that the presence of amphiphilic α-helical potential is present but not conserved in phylogeny within a given protein. The results suggest that the rapid formation of molten globules and the variable behavior of those globules depending on the protein may be a fundamental property of polymers of naturally occurring amino acids more so than a trait that must be derived or maintained by natural selection. Further, the results point toward the utility of randomly occurring process in protein function and evolution, and suggest that the formation of efficient pathways that determine early processes in protein folding, unlike the formation of stable, native protein structure, does not present a substantial hurdle during the evolution of amino acid sequences. Springer Science+Business Media, LLC, 2011 Protein folding nationallicence Helical intermediate nationallicence Evolution nationallicence Amphiphilic nationallicence Randomly occurring processes nationallicence Trifluoroethanol (TFE) nationallicence Lee S. Department of Surgery, Duke University Medical Center, P.O. Box 2605, 27710, Durham, NC, USA aut Parker William Department of Surgery, Duke University Medical Center, P.O. Box 2605, 27710, Durham, NC, USA aut Journal of Molecular Evolution Springer-Verlag 73/3-4(2011-10-01), 166-180 0022-2844 73:3-4<166 2011 73 239 https://doi.org/10.1007/s00239-011-9465-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00239-011-9465-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lee S. Department of Surgery, Duke University Medical Center, P.O. Box 2605, 27710, Durham, NC, USA aut NATIONALLICENCE 700 1- Parker William Department of Surgery, Duke University Medical Center, P.O. Box 2605, 27710, Durham, NC, USA aut NATIONALLICENCE 773 0- Journal of Molecular Evolution Springer-Verlag 73/3-4(2011-10-01), 166-180 0022-2844 73:3-4<166 2011 73 239 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer