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Finkelstein and Badretdinov [A.V. Finkelstein, A.Y. Badretdinov, Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold, Fold. Des. 2 (1997) 115 121] approximated the folding time of protein sequences of length n by exp(λ⋅n2/3±χ⋅n1/2/2)ns, where λ and χ are constants close to unity.
Our results suggest that the kink is conserved in the immunoglobulin heavy chain fold because it disrupts the β-strand pairing at the base of the loop.
This approach allowed us to determine NIR bands, which behave in a way similar to MIR bands originating from conformational defect sequences that exist in the orthorhombic crystalline lattice, the amorphous domain and the chain fold regions.
Inversely, the gene whose expression decreased the most was CD247 (i.e., CD3 zeta chain, fold change −5.19).
Notwithstanding these findings, the results of threading analyses suggest that the entire UPF0201/DUF54 family of archaeal specific proteins share the same overall RRM-type polypeptide chain fold.
We have further documented that all members of this archaeal specific protein family share a common polypeptide chain fold, which is evolutionarily related to the RRM motif found in the ribosomal L5 proteins and many other RNA-binding proteins.
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Electron diffraction indicates that in the whole temperature range, PE crystallizes in flat-on crystals in chain-folded structure with different chain folding stem length.
Increasing BC was found to decrease chain folding and change chain conformation.
The way that the chain folds up might then be predicted.
The latter leads to the average work of chain folding of q̄=7.4±0.8 kcal mol−1.
In this case, the work of chain folding of q̄=9.6±1.1 kcal mol−1 is found.
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