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1 that is composed of alternating hydrophobic/hydrophilic amino acids.
2 butions to protein solubility even among the hydrophilic amino acids.
3 was no consistent selection or expression of hydrophilic amino acids.
4 tely 22% of the transforming proteins lacked hydrophilic amino acids.
5 and binding were mutated to other uncharged, hydrophilic amino acids.
6 by a short lumenal loop of approximately 30 hydrophilic amino acids.
7 ative hydrophobic core of this fragment with hydrophilic amino acids abolished the induced structural
10 umin, biopolymer chains with hydrophobic and hydrophilic amino acids, and (c) DNA fragments, biologic
11 a set of in silico mutations, in which three hydrophilic amino acids are replaced with nonpolar resid
12 ot at all, while changes to smaller and more hydrophilic amino acids are tolerated in both transientl
13 s accomplished by mutation of specific large hydrophilic amino acids (Arg, Gln, Glu, Lys) to Ala, Ser
14 kingly, 35% of the transforming clones had a hydrophilic amino acid at position 17, highlighting the
15 beta receptor and revealed the importance of hydrophilic amino acids at specific positions in the tra
17 have inserted an epitope consisting of eight hydrophilic amino acids (DYKDDDDK) in predicted extracel
18 significantly more favorably than the other hydrophilic amino acids especially at high net charge.
20 To investigate the role of transmembrane hydrophilic amino acids in receptor activation, we const
22 ant residues consist of both hydrophobic and hydrophilic amino acids located at peripheral positions.
23 I, which may explain why AeKAT transaminates hydrophilic amino acids more efficiently than human KAT
24 tioned mostly into the membrane interior and hydrophilic amino acids mostly into the aqueous exterior
26 tch of amino acids on one face of the helix, hydrophilic amino acids on the opposite face, and a numb
28 rane multiple times, with its N-terminal 131 hydrophilic amino acids residing at the cytoplasmic side
29 simply replacing the central hydrophobic or hydrophilic amino acid residue on the nonpolar or the po
30 nd gamma2(L274) subunits were mutated to the hydrophilic amino acid residue serine and coexpressed in
31 The sequence of the peptide is such that hydrophilic amino acid residues at the ends of the other
32 ubstitutions of Thr-888 with hydrophobic and hydrophilic amino acid residues had various effects on C
33 hat the polar 3beta-groups are closer to the hydrophilic amino acid residues in the entrance of the l
34 ly that function in catalysis, the conserved hydrophilic amino acid residues plus a conserved tryptop
36 E5 third transmembrane domain (and terminal hydrophilic amino acids) resulted in a protein with its
37 ides composed of alternating hydrophobic and hydrophilic amino acids self-assemble into amyloid-inspi
38 tructural ordering of vicinal water near the hydrophilic amino acids shifts the equilibrium towards t
40 tide sequence of alternating hydrophobic and hydrophilic amino acids such as VEVE and EVEV self-assem
41 n the ribose 3'- and 5'-substituents and the hydrophilic amino acids T(3.36), S(7.42), and H(7.43), a
42 m using point mutations that converted large hydrophilic amino acids to alanine, yet retained full an
44 ive selection of RF2 that frequently encodes hydrophilic amino acids were noted in the productive rep
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