期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2001
卷号：98
期号：16
页码：9056-9061
DOI：10.1073/pnas.161280798
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The C--H***O hydrogen bond has been given little attention as a determinant of transmembrane helix association. Stimulated by recent calculations suggesting that such bonds can be much stronger than has been supposed, we have analyzed 11 known membrane protein structures and found that apparent carbon hydrogen bonds cluster frequently at glycine-, serine-, and threonine-rich packing interfaces between transmembrane helices. Parallel right-handed helix-helix interactions appear to favor C--H***O bond formation. In particular, C--H***O interactions are frequent between helices having the structural motif of the glycophorin A dimer and the GxxxG pair. We suggest that C--H***O hydrogen bonds are important determinants of stability and, depending on packing, specificity in membrane protein folding.
