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Our finding that the atomic interactions between just 15 20% of residues in native structures of each examined fold are conserved, further suggests that the PCAIN is a minimalistic fold code.
We sought to decode conserved features within each fold family despite the vast degrees of sequence divergence, so as to better understand the factors governing the protein fold code.
PCAIN sheds light on a "fold code" that is consistently encoded into residues that constitute the networks of atomic interactions in solvent unexposed core regions of protein native structures.
This suggests that the fold code is a network phenomenon along with sequence and structural phenomena, thus providing rationale as to why merely sequence-based or structure-based pattern analysis of proteins may not succeed in decoding fold signatures.
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A fourth potential "folding code" (also referred as "stereochemical code") between the translation dynamics, sequence composition and folding of the resulting protein can also be defined in the frame of the 'Anfinsen dogma' followed by post-translational modifications.
However, despite obvious progress in the field and the availability of new technologies and powerful computers, the protein folding code still remains undeciphered.
Folding codes are now being used to successfully design proteins and non-biological foldable polymers; aided by the Critical Assessment of Techniques for Structure Prediction (CASP) competition, protein structure prediction has now become quite good.
Other examples of markedly downregulated genes included SULT1D1 (∼30-fold; coding for sulfotransferase), EPHA7 (∼26-fold; coding for EPH receptor A7), TFCP2L1 (∼15-fold; coding for transcription factor CP2-like 1) and SNCAIP (∼11-fold; coding for synuclein, alpha interacting protein)(Table 4).
All of these data indicate of a degree of informational degeneracy between the sequence and folding codes.
In the mature part of the root, phosphate deficiency induced a high number of genes by more than 4-fold coding for enzymes involved in primary carbon metabolism, i.e. the TCA cycle, glycolysis, Calvin cycle, and mitochondrial ATP synthesis.
Altogether, these findings support a model in which genes can preferentially harbour introns in less constrained regions of the protein fold they code for.
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