Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Anni Kauko"'
Publikováno v:
Protein Science. 23:981-992
The folding of most integral membrane proteins follows a two-step process: initially, individual transmembrane helices are inserted into the membrane by the Sec translocon. Thereafter, these helices fold to shape the final conformation of the protein
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:79-91
Here, we present a study of polar residues within the membrane core of alpha-helical membrane proteins. As expected, polar residues are less frequent in the membrane than expected. Further, most of these residues are buried within the interior of the
Publikováno v:
Journal of Molecular Biology. 380:170-180
With the increasing number of available α-helical transmembrane (TM) protein structures, the traditional picture of membrane proteins has been challenged. For example, reentrant regions, which enter and exit the membrane at the same side, and interf
Autor:
Aron Hennerdal, Anni Kauko, IngMarie Nilsson, Susana Cristobal, Karl Enquist, Mirjam Lerch-Bader, Gunnar von Heijne, Andreas Bernsel, Kristoffer Illergård, Karin Öjemalm, Linnea E. Hedin, Arne Elofsson
Publikováno v:
Journal of Molecular Biology; Vol 396
In mammalian cells, most integral membrane proteins are initially inserted into the endoplasmic reticulum membrane by the so-called Sec61 translocon. However, recent predictions suggest that many transmembrane helices (TMHs) in multispanning membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97ccd5ace88bb829a487f08e25540436
http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-33926
http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-33926