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DB2285 showed a large reduction in A·T binding with a slight enhancement of G·C binding strength such that it had a slight G·C selectivity.
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However, replacement of Asp158 to Phe158 in the cathepsin L 3D structure retained binding of the substrate, with a slight rise of the free energy of binding (-6.1 to - 7.1 kcal/mol).
A158T resulted in a slight increase in F6P binding and a slight decrease in PEP binding.
Polyphenols binding results in a slight secondary structural change of β-Lg, consistent with the fluorescence analysis.
Thermal denaturation, circular dichroism, isothermal titration calorimetry, surface plasmon resonance and DNase I footprinting studies demonstrated that 2 maintained the selectivity of the unlinked parent monomer f-PIP (1) and with a slight enhancement in binding affinity (Keq = 5 × 105 M−1) to the cognate site (5′-TACGAT-3′).
The purified HwHR was adjusted to different chloride concentrations to determine the chloride-binding affinity as described in previous studies with a slight modification [ 19, 20].
The integrin αVβ3 receptor binding study was performed using a previously reported procedure with a slight modification [25].
The binding assay using [125I]α-bungarotoxin was performed as described in a previous report [45] with a slight modification (See Supplemental Method S2).
One of these, R221H, targets a critical residue in the ATP-binding pocket of the protein and causes a severe reduction of α-sarcoglycan, with a slight reduction of the other subunits (Ref. 96).
"No," he said, with a slight smile.
"Always," he said with a slight chuckle.
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