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:1973
卷号:70
期号:5
页码:1456-1460
DOI:10.1073/pnas.70.5.1456
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Conformational energy calculations on thyrotropin releasing factor and on several of its analogues indicate that the central histidyl residue of the native molecule is in an extended conformation. Some derivatives (with a reduced biological activity) have an altered conformation. Since some substitutions leave the conformation unchanged but alter the biological activity, these substitutions must involve the sites responsible for binding of the hormone to its receptor.