{"title":"氢键如何塑造膜蛋白结构。","authors":"Stephen H White","doi":"10.1016/S0065-3233(05)72006-4","DOIUrl":null,"url":null,"abstract":"<p><p>The energetic cost of partitioning peptide bonds into membrane bilayers is prohibitive unless the peptide bonds participate in hydrogen bonds. However, even then there is a significant free energy penalty for dehydrating the peptide bonds that can only be overcome by favorable hydrophobic interactions. Membrane protein structure formation is thus dominated by hydrogen bonding interactions, which is the subject of this review.</p>","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"72 ","pages":"157-72"},"PeriodicalIF":0.0000,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(05)72006-4","citationCount":"36","resultStr":"{\"title\":\"How hydrogen bonds shape membrane protein structure.\",\"authors\":\"Stephen H White\",\"doi\":\"10.1016/S0065-3233(05)72006-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The energetic cost of partitioning peptide bonds into membrane bilayers is prohibitive unless the peptide bonds participate in hydrogen bonds. However, even then there is a significant free energy penalty for dehydrating the peptide bonds that can only be overcome by favorable hydrophobic interactions. Membrane protein structure formation is thus dominated by hydrogen bonding interactions, which is the subject of this review.</p>\",\"PeriodicalId\":51216,\"journal\":{\"name\":\"Advances in Protein Chemistry\",\"volume\":\"72 \",\"pages\":\"157-72\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2005-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0065-3233(05)72006-4\",\"citationCount\":\"36\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Advances in Protein Chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1016/S0065-3233(05)72006-4\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in Protein Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/S0065-3233(05)72006-4","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
How hydrogen bonds shape membrane protein structure.
The energetic cost of partitioning peptide bonds into membrane bilayers is prohibitive unless the peptide bonds participate in hydrogen bonds. However, even then there is a significant free energy penalty for dehydrating the peptide bonds that can only be overcome by favorable hydrophobic interactions. Membrane protein structure formation is thus dominated by hydrogen bonding interactions, which is the subject of this review.