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Showing 1 to 9 of 9 for “"Helix-coil"”.

  1. A Monte Carlo Study of the Helix-Coil Transition

    Made available in DSpace on 2014-12-09T17:35:35Z (GMT). No. of bitstreams: 1 6612404.pdf: 2787704 bytes, checksum: 175cf198fb0837cbb1b50a637a8f3253 (MD5) Previous issue date: 1966

    uiuc Repository record for A Monte Carlo Study of the Helix-Coil Transition (opens in a new tab)

  2. Solvophobically-Driven Folding of Non-Biological Oligomers and the Solid Phase Synthesis of Phenylacetylene Oligomers

    … of helical structure, reversible thermal helix-coil transitions were measured in 4/6, $\rm CH\sb3CN/CHCl\sb3.$ In agreement with the calculations, the octadecamer possesses the largest shift in $\rm\delta\sb{A},$ the best resolved $\sp1$H NMR spectra of the oligomers longer than 12 …

    uiuc Repository record for Solvophobically-Driven Folding of Non-Biological Oligomers and the Solid Phase Synthesis of Phenylacetylene Oligomers (opens in a new tab)

  3. Stapling and Unstapling Peptides and Proteins With S-Tetrazine

    … study a fundamental folding process known as the helix-coil transition by phototriggering coupled with transient two-dimensional infrared spec-troscopy (2D IR). The s-tetrazine molecule possesses the photochemical properties of an ideal phototrigger, as such, s-tetrazine was employed towards the …

    penn Repository record for Stapling and Unstapling Peptides and Proteins With S-Tetrazine (opens in a new tab)

  4. Structural Analysis of an RNA Polymerase Sigma Factor and Its Anti-sigma: sigma28/FLGM

    … The sigma3-sigma4 linker forms a bent α-helix, which is incompatible with the holoenzyme conformation, suggesting that a helix-coil transition may accompany holoenzyme formation. Double cysteine mutants of sigma28, predicted to form interdomain disulfides in this conformation, form even …

    rockefeller Repository record for Structural Analysis of an RNA Polymerase Sigma Factor and Its Anti-sigma: sigma28/FLGM (opens in a new tab)

  5. Using Synthetic Nanopores for Single -Molecule Analyses: Detecting SNPs, Trapping DNA Molecules, and the Prospects for Sequencing DNA

    … which are larger in diameter than the double helix of a DNA molecule but smaller in diameter than the DNA-protein complex. We relate the binding strength to the field threshold at which the complex dissociates. We also describe a method of measuring the transition from double-stranded (dsDNA) …

    uiuc Repository record for Using Synthetic Nanopores for Single -Molecule Analyses: Detecting SNPs, Trapping DNA Molecules, and the Prospects for Sequencing DNA (opens in a new tab)

  6. The α-helical conformation of polypeptides: design, regulation, and applications

    … therefore exhibited reversible, pH-responsive helix-coil transition behavior, which was demonstrated by spectroscopic method, molecular dynamics simulation, as well as small angle neutron scattering technique. The second part of this dissertation focused on the applications of α-helical …

    uiuc Repository record for The α-helical conformation of polypeptides: design, regulation, and applications (opens in a new tab)

  7. Kinesin-1 mechanical flexibility and motor cooperation

    … of kinesin-1 is predicted to be composed of a coiled-coil with two main breaks, the “swivel” (380-442 Dm numbering) and the hinge (560-624). The rotational Brownian motion of microtubules attached to a glass surface by single kinesin molecules was analyzed and measured the torsion elasticity …

    qucosa-diss

  8. The role of interfacial and 'entropic' enzymes in transitory starch degradation : a mathematical modeling approach

    … amylopectin side-chains undergo spontaneous helix-coil transitions. Reversible phosphorylation has a synergistic effect on glucan release especially in the early phase dropping off during degradation. Based on the model, the hypothesis is formulated that interfacial phosphorylation is …

    potsdam-diss Repository record for The role of interfacial and 'entropic' enzymes in transitory starch degradation : a mathematical modeling approach (opens in a new tab)