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As an alternative, one could think of modifying the code of the traditional method to accomodate a target shape p as an extra parameter, and restrict the folding to structures which match p running through list Lenergy.
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(viii)&(v): We have seen in Proposition 2.1 that M † = P ran M * ∘ M - 1 ∘ P ran M. (25).
Then the Moore-Penrose inverse of B satisfies B † = P ran B * ∘ B - 1 ∘ P ran B. (15).
was originally introduced by Euler (for real s) who proved that [[5], p. 1] ζ ( s ) = ∏ p ( 1 - p - s ) - 1 ( where p runs through all primes ), (1.9).
The Ihara zeta function [31] is defined as ∏ p ( 1 − u | p | ) − 1, where p runs over all closed prime paths in the graph and | p | is its length.
Let H ( R n ) + ⊂ H ( R n ) be the (normal) subgroup generated by the R u ( P ) ( R n ) where P runs over the set of parabolic subgroups of H considered in Theorem 12.1.
The interpolation parameter p runs from 0.0 to 3.0 and the parameter sets from Appendix are located at p=0.0,1.0, and 2.0, respectively.
Experiments were performed at 25°C and 30 µl/min using HBS-P running buffer (0.01 M HEPES pH 7.4, 0.15 M NaCl and 0.005% surfactant P20) (Biacore).
The dissociation duration for bound analytes was 15 minutes in HBS-P running buffer (10 mM HEPES, pH 7.4, 150 mm NaCl and 0.005% surfactant P20, filtered and degassed).
Enzyme was added to RNP total protein in HBS-P running buffer to a final concentration of 4.8 U/ml.
Complete peptide sequences were as follows: N: DTDTPIVYNDRNLLD N4D: DTDTPIVYNDR DLLD N3PD: DTDTPIVYNDR DPLD p53: STSRHKKLMFKTEGP MBP: YGSLPQKAQRPQDEN Binding reactions were performed in HBS-P running buffer (0.01 M HEPES pH 7.4, 0.15 M NaCl, 0.005% Surfactant P20) adjusted to a final concentration of 2.5 mM MgAcetate and 2.5 mM ATP (Disodium Salt, Sigma).
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