Sentence examples for shift of residue from inspiring English sources

For each amino acid μ, it is possible to define the difference between observed and predicted Cαchemical-shifts as: (1) where, Cμ, i α is the chemical shift of residue μ in conformation i out of Ω conformations.

The map also suggests a register shift of residues 1,061 1,079 on M13 in the structure by another group (PDB: 6BAA) (Martin et al., 2017a).

The flap is slightly more compact in PKAc ADP psSP20 due to a 1.5 Å shift of residues 52 54 away from the alternate conformation of thiophosphate side chain of psSer21SP20.

Membrane association of α-Synuclein has been described as a two-step process with binding of amino acids 3 25 followed by a conformational shift of residues 26 100 into a α-helical structure which cooperatively binds to the membrane [ 4, 8].

The carbonyl moiety of Thr379 in complexed TmPurL, which forms a hydrogen bond with the main chain amide of Arg393, is responsible for the shift of residues 390−395, located in a loop, closer to the long linker region.

At the same time, there appears to be a slight decrease in helicity at the C-terminal end of the H helix, as indicated by a decrease in the secondary chemical shift of residues D141, I142, and Y146.

Specifically, chemical shifts of residues 7 16 are again shifted by ∼0.5 ppm on average.

Excellent agreement is observed between excited state chemical shifts of residues selected as part of process I, from analysis of CEST data, and the previously reported (Banci et al., 2002a) ground state chemical shifts of dimer interface residues in Cu2Zn2SOD1S S.

In particular, chemical shifts of residues in α1, α2, and L4 showed significant perturbations, indicating that this region is likely the site of interaction.

Most notable were changes in amide H/N chemical shifts of residues F12, W18, N19, T20, F52, and Q86, residues primarily within or adjacent to RNP1 and RNP2 consensus RNA-binding sequence sites.

Although the effect of N-terminal acetylation on the chemical shifts of residues 6 12 rapidly decreases with the distance from the N-terminus, it is rather remarkable that the effect of this small covalent modification in a disordered protein propagates as far as residue 12, an effect explained by the cooperative formation of a transient short α-helix of the N-terminal residues.