Folding, structure and evolution of integral alpha helical membrane proteins


Project leader


Funding source

Swedish Research Council - Vetenskapsrådet (VR)


Project Details

Start date: 01/01/2009
End date: 31/12/2011
Funding: 2700000 SEK


Description

In this application we focus on improve the understanding of the structure and folding of membrane proteins. Traditionally it has been assumed that the membrane proteins fold in a two-step procedure, where the recognition of sufficiently hydrophobic TM helices is followed by a simple folding process where these helices pack optimally. However, we, and others, have in a number of recent studies shown that this simple picture is incomplete. Here, we aim to gain further insights into this process, using a multi-disciplinary approach combining bioinformatical and experimental studies with three main components, (i) structural and evolutionary analysis of TM proteins (ii) development of novel methods to predict features of these proteins and (iii) study the insertion of different proteins, and parts of proteins, into the membrane using a well established microsomal system. In addition to the use of these well-established techniques we plan to increase our portfolio of methods mainly through collaborations, see details below. By a combination of these approaches we will focus on four related sub-projects: (a) Translocon recognition of marginally hydrophobic helices (b) Identifying 2.5 D features of TM-proteins (c) Studies of post-translational rearrangements during membrane protein folding (d) Conserved of topology throughout evolution ?

Last updated on 2017-31-03 at 12:59