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Young, Jason - - 2010
Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their ...
Cloutier, Philippe - - 2010
More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, ...
Sweeting, B. - - 2010
The term prion disease describes a group of fatal neurodegenerative diseases that are believed to be caused by the pathogenic misfolding of a host cell protein, PrP. Susceptibility to prion disease differs between species and incubation periods before symptom onset can change dramatically when infectious prion strains are transmitted between ...
Rauscher, Sarah - - 2010
Protein disorder is abundant in proteomes throughout all kingdoms of life and serves many biologically important roles. Disordered states of proteins are challenging to study experimentally due to their structural heterogeneity and tendency to aggregate. Computer simulations, which are not impeded by these properties, have recently emerged as a useful ...
Rutledge, Angela - - 2010
Apolipoprotein B100 (apoB) is a large amphipathic lipid-binding protein that is synthesized by hepatocytes and used to assemble and stabilize very low density lipoproteins (VLDL). It may have been derived through evolution from other lipid-associating proteins such as microsomal triglyceride transfer protein or vitellogenin. The correct folding of apoB requires ...
Tompa, Peter - - 2010
Intrinsically disordered proteins (IDPs) are widespread in eukaryotes and fulfill important functions associated with signaling and regulation. Recent evidence points to a special and thus largely disrespected functional capacity of IDPs--that they can assist the folding of other proteins and prevent their aggregation, i.e., that they can act as chaperones. ...
Ng, Derek - - 2010
In studies of the structural biology of membrane proteins, the success of strategies based on the "divide and conquer" approach, where peptides are used to model the individual transmembrane (TM) [alpha]-helices of membrane proteins, depends on the correct identification of the membrane-embedded TM [alpha]-helix amino acid sequence within the full-length ...
Muiznieks, Lisa - - 2010
Elastin is a self-assembling, extracellular-matrix protein that is the major provider of tissue elasticity. Here we review structural studies of elastin from over four decades, and draw together evidence for solution flexibility and conformational disorder that is inherent in all levels of structural organization. The characterization of disorder is consistent ...
Clark, Gregory - - 2010
GroEL is a chaperone thought of as essential for bacterial life. However, some species of Mollicutes are missing GroEL. We use phylogenetic analysis to show that the presence of GroEL is polyphyletic among the Mollicutes, and that there is evidence for lateral gene transfer of GroEL to Mycoplasma penetrans from ...
Wathen, Brent - - 2010
The [alpha]-helix remains a focus of research because of its importance to protein folding and structure. Nevertheless, despite numerous empirical, computational, and theoretical studies, the fundamental structural properties governing their formation and stability are still unclear. We have examined the statistical occurrence of polar and apolar residue patterning in helical ...
Duvignaud, Jean-Baptiste - - 2010
The Core protein of hepatitis C virus is involved in several interactions other than the encapsidation of viral RNA. We recently proposed that this is related to the fact that the N-terminal half of this protein (C82) is an intrinsically unstructured protein (IUP) domain. IUP domains can adopt a secondary ...
Zarrine-Afsar, Arash - - 2010
Understanding how proteins adopt their unique native structures requires a complete structural characterization of the rate-limiting transition state(s) along the folding pathway. By definition, transition states are not significantly populated and are only accessible via folding kinetics studies. In this respect, interpreting the kinetic effects of amino acid substitutions (especially ...
Reddy, Tyler - - 2010
Biomolecular nuclear magnetic resonance (NMR) spin relaxation experiments provide exquisite information on the picosecond to nanosecond timescale motions of bond vectors. Spin-lattice ([T.sub.1]) and spin-spin ([T.sub.2]) relaxation times and the steady-state nuclear Overhauser effect (NOE) are the first set of parameters extracted from typical [sup.15]N or [sup.13]C NMR relaxation experiments. ...
Langelaan, David - - 2010
The membrane catalysis hypothesis states that a peptide ligand activates its target receptor after an initial interaction with the surrounding membrane. Upon membrane binding and interaction, the ligand is structured such that receptor binding and activation is encouraged. As evidence for this hypothesis, there are numerous studies concerning the conformation ...
Stathopulos, Peter - - 2010
Spatiotemporally discrete cytoplasmic [Ca.sup.2+] fluctuations are fundamental eukaryotic signals in myriad physiological and pathophysiological functions. Store-operated [Ca.sup.2+] entry is the process whereby a decrease in endoplasmic reticulum (ER) luminal [Ca.sup.2+] levels activates [Ca.sup.2+] release activated calcium (CRAC) channels on the plasma membrane (PM), providing a sustained [Ca.sup.2+] elevation to the ...
Johnson, Jadah - - 2010
Cysteine string protein (CSP[alpha], also called DnaJC5) is unique among J proteins. Similar to other J proteins, CSP[alpha] interacts with and activates the ATPase of Hsc70s (heat shock proteins of 70 kDa), thereby harnessing the ATPase activity for conformational work on client proteins. In contrast to other J proteins, CSP[alpha] ...
Libich, David - - 2010
The classic 18.5 kDa isoform of myelin basic protein (MBP) is central to maintaining the structural homeostasis of the myelin sheath of the central nervous system. It is an intrinsically disordered, promiscuous, multifunctional, peripheral membrane protein, whose conformation adapts to its particular environment. Its study requires the selective and complementary ...
Hoover, Todd - - 2010
Rubenstein, David - - 2010
Perry, Ann - - 2010
Bliss, Rosalie - - 2010
Durham, Sharon - - 2010
Spence, Joseph - - 2010
Angelou, Maya - - 2010
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