... molecular chaperones protein folding single-molecule force spectroscopy single-molecule FRET The 70-kDa heat shock proteins (Hsp70s) form the central hub of the proteostasis network, which is involved in a number of cellular processes, including assisting the folding of nascent peptide chains...

... Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) . co-translational folding lipids membrane proteins protein folding Membrane proteins reside in a chemically complex environment. They must interact...

... the Creative Commons Attribution License 4.0 (CC BY) . dopamine transporter pharmacochaperoning protein folding serotonin transporter Transporters for the monoamines norepinephrine (NET), serotonin (SERT) and dopamine (DAT) belong to the SLC6 (solute carrier 6) transporter family. All SLC6...

... ), where helices can interact with each other and with the membrane before translation is complete (ribosome not shown). The majority of work on membrane protein folding uses relatively well-behaved proteins that have been purified following cellular overexpression and partially unfolded...

... phenotype protein folding self-assembly Silk has for some time been one of the much heralded success stories of Bio-Engineering with dope expression in potatoes [ 1 ] various microbes [ 2 ] and even goat-milk [ 3 ] some with names like Bio-Steel™ to market the fibrous product. Yet none...

...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. © The Authors Journal compilation © 2015 Biochemical Society 2015 free energy landscape pre-exponential factor protein folding reaction coordinate 1 To whom correspondence should be addressed (email...

...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...

... protein folding slipknotted protein For a long time, it was believed that knots were too complicated to exist in protein structures [ 1 ]. The situation changed in 2000 [ 2 ] when the first deeply embedded protein knot was discovered. Since then, knots and slipknots (slipknots arise from...

...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. amino acid cluster Im protein kinetic intermediate state (KIS) NMR protein folding Knowledge of protein structures is a central feature...

.... Cristobal S. Elofsson A. von Heijne G. Repositioning of transmembrane α-helices during membrane protein folding J. Mol. Biol. 2010 397 190 201 16 Zhang L. Sato Y. Hessa T. von Heijne G. Lee J.K. Kodama I. Sakaguchi M. Uozumi N. Contribution...

...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...

... form. Knowledge of the structure of amyloid fibrils is of interest both medically and for our understanding of protein folding and misfolding. Understanding at an atomic level can give insights into mechanisms of assembly and provide the ability to exploit any resulting rules. The structure...

... Biochemical Society 2009 aggregation β-sheet insulin nanoparticle protein folding spherulite The second aggregate structure is that which we have termed a spherulite [ 3 ], because of its similarity under the polarizing microscope to the semi-crystalline structures seen in synthetic...

... correspondence should be addressed (email [email protected] ). 1 7 2005 © 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...

... 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 lectin chaperones calnexin...

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