{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T14:25:12Z","timestamp":1770474312684,"version":"3.49.0"},"reference-count":47,"publisher":"Proceedings of the National Academy of Sciences","issue":"5","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2001,2,27]]},"abstract":"<jats:p>\n            Although many polar residues are directly involved in transmembrane\n protein functions, the extent to which they contribute to more general\n structural features is still unclear. Previous studies have\n demonstrated that asparagine residues can drive transmembrane helix\n association through interhelical hydrogen bonding [Choma, C.,\n Gratkowski, H., Lear, J. D. &amp; DeGrado, W. F. (2000)\n            <jats:italic>Nat. Struct. Biol.<\/jats:italic>\n            7, 161\u2013166; and Zhou, F. X.,\n Cocco, M. J., Russ, W. P., Brunger, A. T. &amp; Engelman,\n D. M. (2000)\n            <jats:italic>Nat. Struct. Biol.<\/jats:italic>\n            7, 154\u2013160]. We have\n studied the ability of other polar residues to promote helix\n association in detergent micelles and in biological membranes. Our\n results show that polyleucine sequences with Asn, Asp, Gln, Glu, and\n His, residues capable of being simultaneously hydrogen bond donors and\n acceptors, form homo- or heterooligomers. In contrast, polyleucine\n sequences with Ser, Thr, and Tyr do not associate more than the\n polyleucine sequence alone. The results therefore provide experimental\n evidence that interactions between polar residues in the helices of\n transmembrane proteins may serve to provide structural stability and\n oligomerization specificity. Furthermore, such interactions can allow\n structural flexibility required for the function of some membrane\n proteins.\n          <\/jats:p>","DOI":"10.1073\/pnas.041593698","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:45:09Z","timestamp":1027694709000},"page":"2250-2255","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":301,"title":["Polar residues drive association of polyleucine transmembrane helices"],"prefix":"10.1073","volume":"98","author":[{"given":"Fang Xiao","family":"Zhou","sequence":"first","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale\r University, New Haven, CT 06520-8114; Department of\r Chemistry, Yale University, New Haven, CT 06520; and\r Department of Molecular and Cellular Physiology,\r Department of Neurology and Neurological Sciences, and\r Howard Hughes Medical Institute, Stanford University,\r Stanford, CA 94305"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Helen J.","family":"Merianos","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale\r University, New Haven, CT 06520-8114; Department of\r Chemistry, Yale University, New Haven, CT 06520; and\r Department of Molecular and Cellular Physiology,\r Department of Neurology and Neurological Sciences, and\r Howard Hughes Medical Institute, Stanford University,\r Stanford, CA 94305"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Axel T.","family":"Brunger","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale\r University, New Haven, CT 06520-8114; Department of\r Chemistry, Yale University, New Haven, CT 06520; and\r Department of Molecular and Cellular Physiology,\r Department of Neurology and Neurological Sciences, and\r Howard Hughes Medical Institute, Stanford University,\r Stanford, CA 94305"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donald M.","family":"Engelman","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale\r University, New Haven, CT 06520-8114; Department of\r Chemistry, Yale University, New Haven, CT 06520; and\r Department of Molecular and Cellular Physiology,\r Department of Neurology and Neurological Sciences, and\r Howard Hughes Medical Institute, Stanford University,\r Stanford, CA 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