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1 lanthanide series, underscoring an intrinsic nonequivalence.
2 th the kinetic data that demonstrate induced nonequivalence and cooperativity of OPRTase.
3                      We uncovered functional nonequivalence between RUNX paralogs.
4 ndom marker distribution can account for the nonequivalence between the number of linkage groups and
5 oline moieties generally produce the largest nonequivalence in the 1H NMR spectra of the substrates.
6                      These results suggest a nonequivalence in the binding interaction at the two sit
7                                         This nonequivalence is a direct result of the specific functi
8  3, 3(2-), and 3(2-)/2K(+) indicate that the nonequivalence is due to both slow rotation across a bar
9 st-translational modification highlights the nonequivalence of human Hb alpha, beta, and gamma subuni
10 genomes fail early in development due to the nonequivalence of parental genomes caused by genomic imp
11 elated ion channels and about the functional nonequivalence of subunits with identical amino acid seq
12 ts, together with kinetic findings, indicate nonequivalence of subunits within a MutS oligomer with r
13 n of our observational study is the possible nonequivalence of the cohorts, particularly the 4.5- to
14 y at the third Asn67 site is a result of the nonequivalence of the glycoprotein environments, leaving
15                   This is complicated by the nonequivalence of the human and mouse FPR gene families
16                                          The nonequivalence of the regulatory patterns in the wild-ty
17 nly a single heteroduplex molecule, implying nonequivalence of the two dimers within the tetramer.
18 f these findings confirms the conformational nonequivalence of the two nucleotide-binding sites in th
19 s in the X versus Y position, related to the nonequivalence of these positions in terms of interchain
20 In vitro and in vivo experiments suggest the nonequivalence of these sites and the potential importan
21                                  The dynamic nonequivalence of two, otherwise chemically equivalent,
22 elps solve the problem of the chemical shift nonequivalences of nonprotonated aromatic carbons in pro
23                                         This nonequivalence reaches its pinnacle in the mammalian bet
24  conformer with an (S)-configuration and the nonequivalence sense of the tert-butyl group chemical sh
25 heritance are not equivalent and to use this nonequivalence to test for deviations from simple models