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1 peptide, contains a high ratio of charged to hydrophobic amino acid residues.
2 acid residues 154-193), which contains many hydrophobic amino acid residues.
3 f its heptad a positions are not occupied by hydrophobic amino acid residues.
4 ce showed a clear demarcation of charged and hydrophobic amino acid residues.
5 ts the solvent-mediated interactions between hydrophobic amino-acid residues.
8 d a conserved C-terminal primary anchor with hydrophobic amino acid residues, as well as one or more
9 nstitutive activity, suggesting that a large hydrophobic amino acid residue at position 254 alters tr
11 lycosylhydrolases, including both acidic and hydrophobic amino acid residues critical for enzyme acti
12 promoters; (ii) assess the role of conserved hydrophobic amino acid residues for MarA activity; and (
16 interactions of Arg120, Tyr355, and several hydrophobic amino acid residues in the COX-2 active site
17 s in mussel plaques), the high proportion of hydrophobic amino acid residues in the flanking sequence
19 conserved CxxxC motif (where "x" can be any hydrophobic amino acid residue) in physical interactions
20 roduction of highly fluorinated analogues of hydrophobic amino acid residues into proteins has proved
21 ional analyses revealed that three blocks of hydrophobic amino acid residues located within TAND3 are
22 Ga-Pa-PCNA1 complex is thermostable, and two hydrophobic amino acid residues on Pa-UDGa (Phe(191) and
25 tween helices of a coiled coil are formed by hydrophobic amino acid residues packed in a "knobs-into-
27 ccurs primarily through aromatic, basic, and hydrophobic amino acid residues, the majority of which a
28 te-directed mutagenesis to change charged or hydrophobic amino acid residues to alanines to identify
29 that this leucine may interact with several hydrophobic amino acid residues to influence the spatial
30 or silk proteins is a strong predominance of hydrophobic amino acid residues to provide for the hydro
32 viously suggested role of a stretch of small hydrophobic amino acid residues within the first transme
33 on defects resulted solely from mutations of hydrophobic amino acid residues within the hydrophobic c
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