temporary banners

 



 

Journal Issue - Volume 2 Issue 12 (December 1993)

Abstract NMR studies are now unraveling the structure of intermediates of protein folding using hydrogen—deuterium exchange methodologies. These studies provide information about the time dependence of formation of secondary structure. They require the ability to assign specific resonances in the NMR spectra to specific amide protons of a protein followed by experiments involving competition between folding and exchange reactions....

  • Sequence‐specific

  • C.M. Fletcher, R.A. Harrison, P.J. Lachmann, D. Neuhaus
  • Published in Wiley Interscience on Dec 31, 2008
  • DOI: 10.1002/pro.5560021203 (p 2015-2027)

Abstract CD59 is a recently discovered cell‐surface glycoprotein that restricts lysis by homologous complement and has limited sequence similarity to snake venom neurotoxins. This paper describes the first results of a two‐dimensional NMR study of CD59 prepared from human urine. Nearly complete 1H‐NMR assignments were obtained for the 77 amino acid residues and partial assignments for the N‐glycan and the glycosylphosphatidylinositol ...

  • Thermodynamics of bpti folding

  • George I. Makhatadze, Key‐Sun Kim, Clare Woodward, Peter L. Privalov
  • Published in Wiley Interscience on Dec 31, 2008
  • DOI: 10.1002/pro.5560021204 (p 2028-2036)

Abstract A calorimetric study of the basic pancreatic trypsin inhibitor (BPTI) has been performed using the new generation of the adiabatic scanning microcalorimeters, operating in an extended temperature range of 5–130 °C. Precise measurements of the heat capacities of the native and unfolded states of BPTI show that the heat capacity change upon unfolding strongly depends on temperature; its value is maximal at about 50 °C and...

Abstract We have used thermal and chemical denaturation to characterize the thermodynamics of unfolding for turkey ovomucoid third domain (OMTKY3). Thermal denaturation was monitored spectroscopically at a number of wavelengths and data were subjected to van't Hoff analysis; at pH 2.0, the midpoint of denaturation (Tm) occurs at 58.6 + 0.4 °C and the enthalpy of unfolding at this temperature (ΔHm) is 40.8 + 0.3 kcal/mol. When Tm was perturbed...

Abstract How important are helical propensities in determining the conformations of globular proteins? Using the two‐dimensional lattice model and two monomer types, H (hydrophobic) and P (polar), we explore both nonlocal interactions, through an HH contact energy, as developed in earlier work, and local interactions, through a helix energy, σ. By computer enumeration, the partition functions for short chains are obtained without approximation...

Abstract N‐Methyl‐d‐aspartate (NMDA) receptor subunits were characterized with seven polyclonal antibodies. The antibodies were directed against NR1‐A, NR2A‐N1, and NR2C‐N1, representing N‐terminal sequences of the NR1, NR2A, and NR2C subunits, and against NR1‐E, NR2A‐C1, and NR2C‐C1, derived from C‐terminal sequences of these subunits. The anti‐NR1‐D antibody was raised against the putative internal loop of NR1. ...

Abstract Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients across the cell membranes of many bacteria, fungi, and some tumor cells, although it does not lyse red blood cells. One‐ and two‐dimensional solid‐state 15N NMR spectra of specifically 15N‐labeled magainin 2 in oriented bilayer samples show that the secondary...

Abstract The glutathione S‐transferase (GST) isoenzyme A1–1 from rat contains a single tryptophan, Trp 21, which is expected to lie within α‐helix 1 based on comparison with the X‐ray crystal structures of the pi‐ and mu‐class enzymes. Steady‐state and multifrequency phase/modulation fluorescence studies have been performed in order to characterize the fluorescence parameters of this tryptophan and to document ligand‐induced conformational...

Abstract MIF proteins are mammalian polypeptides of approximately 13, 000 molecular weight. This class includes human macrophage migration inhibitory factor (MIF), a rat liver protein that has glutathione S‐transferase (GST) activity (TRANSMIF), and the mouse delayed early response gene 6 (DER6) protein. MIF proteins were previously linked to GSTs by demonstrating transferase activity and observing N‐terminal sequence homology with a mu‐class...

Abstract Monoclonal antibodies that bind native protein can generate considerable information about structure/function relationships, but identification of their epitopes can be problematic. Previously, monoclonal antibody M8‐P1‐A3 has been shown to bind to the catalytic (α) subunit of the Na+, K+‐ATPase holoenzyme and the synthetic peptide sequence 496‐HLLVMK*GAPER‐506, which includes Lys 501 (K*), the major site for...

Abstract The structure of phthalate dioxygenase reductase (PDR), a monomeric iron‐sulfur flavoprotein that delivers electrons from NADH to phthalate dioxygenase, is compared to ferredoxin‐NADP+ reductase (FNR) and ferredoxin, the proteins that reduce NADP+ in the final reaction of photosystem I. The folding patterns of the domains that bind flavin, NAD(P), and [2Fe‐2S] are very similar in the two systems. Alignment of the X‐ray structures of...

Abstract Efforts to predict protein secondary structure have been hampered by the apparent structural plasticity of local amino acid sequences. Kabsch and Sander (1984, Proc. Natl. Acad. Sci. USA 81, 1075–1078) articulated this problem by demonstrating that identical pentapeptide sequences can adopt distinct structures in different proteins. With the increased size of the protein structure database and the availability of new methods to...

Abstract A classification is presented of doubly wound α/β nucleotide binding topologies, whose binding sites are located in the cleft formed by a topological switch point. In particular, the switch point loop nearest the N‐terminus is used to identify specific structural classes of binding protein. This yields seven structurally distinct loop conformations, which are subsequently used as motifs for scanning the Protein Data Bank. ...

Abstract The αIIbβ3 platelet integrin is the prototypical member of a widely distributed class of transmembrane receptors formed by the noncovalent association of α and β subunits. Electron microscopic (EM) images of the αIIbβ3 complex show an asymmetric particle with a globular domain from which two extended regions protrude to contact the lipid bilayer. Distance constraints provided by disulfide bond patterns, epitope mapping, and ligand...

Page:   1 2 Next