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It has been illustrated that the single-lattice-cell method is not sufficiently accurate for heterogeneous core configurations when adjacent channels experience significant spectrum interaction.
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Here we review recent progress in the understanding of quasispecies dynamics, notably the occurrence of intra-mutant spectrum interactions, and implications of fitness landscapes for virus adaptation and de-adaptation.
The viral macrophage inflammatory protein II (vMIP-II) which showed a broad-spectrum interaction with both CC and CXC chemokine receptors including CCR5 and CXCR4, two principal coreceptors for the cell entry of human immunodeficiency virus.
Elucidating the events during appressoria formation could shed light on the mechanism allowing broad-spectrum interaction.
The viral macrophage inflammatory protein-II (vMIP-II) encoded by Kaposi's sarcoma-associated herpesvirus is unique among all known chemokines, in that vMIP-II shows a broad-spectrum interaction with both CC and CXC chemokine receptors including CXCR4 (Kledal et al, 1997).
Genes that function in the same pathways show consistent, suppressive genetic interactions across a spectrum of interaction partners.
Quantitative bioactivity assays provide convenient data that capture the whole spectrum of interaction affinities, including both true-positive and -negative interactions.
We argue that the experimental data sets of Kd/Ki or other bioactivity measurements provide more realistic response variable for the prediction problem in terms of representing the whole spectrum of interaction affinities, including both true-positive and -negative interactions.
The spectrum load interaction models used in these programs are examined in some detail.
The FT-IR spectra showed that the peak positions of amide I bands shifted from 1656.40 to 1637.83 cm−1 in HSA infrared spectrum after interaction with glycyrrhetinic acid.
More specifically, this analysis is not meant to uncovering the full spectrum of interaction patterns among mutations.
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