onr:"swepub:oai:DiVA.org:su-119748"
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03215naa a2200373 4500 | |
| 001 | oai:DiVA.org:su-119748 | |
| 003 | SwePub | |
| 008 | 150824s2015 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1197482 URI |
| 024 | 7 | a https://doi.org/10.1002/pro.26982 DOI |
| 040 | a (SwePub)su | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a for2 swepub-publicationtype |
| 100 | 1 | a De Marothy, Minttu T.u Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)4 aut0 (Swepub:su)mivi3794 |
| 245 | 1 0 | a Marginally hydrophobic transmembrane alpha-helices shaping membrane protein folding |
| 264 | c 2015-05-30 | |
| 264 | 1 | b Wiley,c 2015 |
| 338 | a electronic2 rdacarrier | |
| 520 | a Cells have developed an incredible machinery to facilitate the insertion of membrane proteins into the membrane. While we have a fairly good understanding of the mechanism and determinants of membrane integration, more data is needed to understand the insertion of membrane proteins with more complex insertion and folding pathways. This review will focus on marginally hydrophobic transmembrane helices and their influence on membrane protein folding. These weakly hydrophobic transmembrane segments are by themselves not recognized by the translocon and therefore rely on local sequence context for membrane integration. How can such segments reside within the membrane? We will discuss this in the light of features found in the protein itself as well as the environment it resides in. Several characteristics in proteins have been described to influence the insertion of marginally hydrophobic helices. Additionally, the influence of biological membranes is significant. To begin with, the actual cost for having polar groups within the membrane may not be as high as expected; the presence of proteins in the membrane as well as characteristics of some amino acids may enable a transmembrane helix to harbor a charged residue. The lipid environment has also been shown to directly influence the topology as well as membrane boundaries of transmembrane helices-implying a dynamic relationship between membrane proteins and their environment. | |
| 650 | 7 | a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng |
| 653 | a membrane protein folding | |
| 653 | a hydrophobicity | |
| 653 | a marginally hydrophobic transmembrane helices | |
| 653 | a aquaporin 1 | |
| 700 | 1 | a Elofsson, Arneu Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)4 aut0 (Swepub:su)aelof |
| 710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
| 773 | 0 | t Protein Scienced : Wileyg 24:7, s. 1057-1074q 24:7<1057-1074x 0961-8368x 1469-896X |
| 856 | 4 | u https://su.diva-portal.org/smash/get/diva2:849160/FULLTEXT01.pdfx primaryx Raw objecty fulltext:preprint |
| 856 | 4 | u https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/pro.2698 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-119748 |
| 856 | 4 8 | u https://doi.org/10.1002/pro.2698 |
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