... BY) . co-translational folding lipids membrane proteins protein folding Membrane proteins reside in a chemically complex environment. They must interact with the hydrophobic bilayer interior and the aqueous environment outside the bilayer, as well as the interface between the two. The final...

... the Creative Commons Attribution License 4.0 (CC BY) . dopamine transporter pharmacochaperoning protein folding serotonin transporter Fröhlich and Loewi discovered that cocaine potentiated of the action of adrenaline already at the beginning of the 20th century [ 11 ], but it took another 50...

... of membrane proteins, including folding rate, yield, topology and stability have dissimilar dependences on lipid headgroup charge and lateral pressure. lipid bilayer lipid composition protein folding transmembrane proteins Membrane proteins comprise over a third of proteins in the cell...

... body morphology. 1 email fritz.vollrath@zoo.ox.ac.uk 9 2 2016 © 2016 The Author(s). published by Portland Press Limited on behalf of the Biochemical Society 2016 anticipatory molecules emergent properties extended phenotype protein folding self-assembly Silk has...

...Jim E. Horne; Sheena E. Radford Great strides into understanding protein folding have been made since the seminal work of Anfinsen over 40 years ago, but progress in the study of membrane protein folding has lagged behind that of their water soluble counterparts. Researchers in these fields...

...Pamela J.E. Rowling; Elin M. Sivertsson; Albert Perez-Riba; Ewan R.G. Main; Laura S. Itzhaki Studying protein folding and protein design in globular proteins presents significant challenges because of the two related features, topological complexity and co-operativity. In contrast, tandem-repeat...

... coordinate, and its application to the analysis of simulated protein folding dynamics. 1 To whom correspondence should be addressed (email p.banushkina@leeds.ac.uk ). 22 9 2014 © The Authors Journal compilation © 2015 Biochemical Society 2015 free energy landscape pre-exponential...

...David Baker I describe how experimental studies of protein folding have led to advances in protein structure prediction and protein design. I describe the finding that protein sequences are not optimized for rapid folding, the contact order–protein folding rate correlation, the incorporation...

... effect of topology on the folding route. Figure 2 Comparison of free energy landscapes of a structurally similar hypothetical protein MJ0366 ( A ) and VirC2 ( B ) (PDB codes 2EFV and 2RH3 respectively) The proteins fold the β-sheet first, which defines the twisted-loop intermediate that precedes...

...Andrzej Stasiak; Andrew D. Bates; Dorothy E. Buck; Sarah A. Harris; De Witt Sumners The Topological Aspects of DNA Function and Protein Folding international meeting provided an interdisciplinary forum for biological scientists, physicists and mathematicians to discuss recent developments...

... protein. We suggest that this kind of alignment is present in other proteins and is relevant to how native state topology determines folding rates. 8 9 2011 amino acid cluster Im protein kinetic intermediate state (KIS) NMR protein folding Knowledge of protein structures...

...., how membrane proteins fold and oligomerize that have so far been almost universally ignored. We still have a long way to go before we can confidently say that we understand these greasy little beasts sufficiently well to put them to rest with a contented smile on our face . Recent Advances...

...Peter Lund It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding...

... compilation © 2009 Biochemical Society 2009 amyloid assembly β-sheet cross-β diffraction fibre protein folding Figure 3 Cross-β diffraction pattern and structure ( a ) The cross-β diffraction pattern observed for amyloid fibrils, taken from fibrils formed by Sup35 NM [ 47 ]. Arrows...

... nanoparticle protein folding spherulite Bionanotechnology II: from Biomolecular Assembly to Applications: Biochemical Society Focused Meeting held at Robinson College, Cambridge, U.K., 7–9 January 2009. Organized and Edited by Tony Cass (Imperial College London, U.K.) and Dek Woolfson (Bristol...

... strain 79A; lane 3, sporadic CJD (Creutzfeldt–Jacob disease); and lane 4, variant CJD. © 2005 The Biochemical Society 2005 Creutzfeldt–Jacob disease (CJD) glycosylation prion protein folding PrP transmissible spongiform encephalopathy (TSE) Prusiner first proposed the prion...

...S. Dias-Gunasekara; A.M. Benham The ER (endoplasmic reticulum) is the site of protein folding for all eukaryotic secreted and plasma membrane proteins. Disulphide bonds are formed in many of these proteins through a dithiol–disulphide exchange chain comprising two types of protein catalysts: PDI...

... and chaperone activities is probably what makes PDI an effective and generally important enzyme in oxidative protein folding [ 8 ]. ERp57 differs from PDI by catalysing disulphide bond formation almost exclusively in glycoproteins [ 9 , 10 ], a function that is achieved through its interaction with the two...

... in this new membrane protein insertion pathway. 1 To whom correspondence should be addressed (e-mail tokatlidis@man.ac.uk ) 7 3 2000 © 2000 Biochemical Society 2000 chaperones metabolite carriers protein folding protein targeting AAC, mitochondrial ADP/ATP carrier PiC...