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The spontaneous formation of double helices for filaments under torsion is common and significant.
Here, we used yeast display to screen a library of grafted C-peptide helices for N-peptide trimer recognition.
Therefore an ideal model was presented to investigate the formation of double helices for elastic rods under torque.
We have developed a computational method for predicting recognition helices for C2H2 zinc fingers that bind to specific target DNA sites.
Based on this rule, we developed score functions and automated methods for orienting TM helices, for which locations and tilt angles have been determined using, e.g., cryo-EM data.
RolR is an all-helix protein and each subunit is composed of 9 α helices (h1, h2, h4 h10) and two 310 helices for h3 and g1, a stretch between h1 and h2 (Fig. 1).
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In addition, molecular dynamics simulations suggest equilibrium between dimers, trimers, and tetramers of α-helices for peptide B.
By deriving differential geometric parameters from these models one obtains a reliable method to characterize and compare α-helices for a broad range of applications.
As a model of the protein targets for volatile anesthetics, the dimeric four-α-helix bundle, (Aα2-L1M/L38M 2, was designed to contain a long hydrophobic core, enclosed by four amphipathic α-helices, for specific anesthetic binding.
Oxaldie-3 was an efficient catalyst at concentrations as low as 2 μM, 100-fold lower than the previously described Oxaldie-2, which relied on aggregating α-helices for activity.
There are hydrophobic contacts between the two α-helices, for example, Leu233 in helix-1 with Ile253 in helix-2.
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