Sentence examples for binding residues is based from inspiring English sources

The use of models for predicting binding residues is based on an inherent assumption that a protein is known to bind DNA.

Originally, the definition of sequence-specific binding and the non-specific binding residues is based on the identification of hydrogen bonds and van der Waals attractions between protein side-chains and DNAs.

The role for non-specific binding residues is to stabilize the interactions between protein and nucleotide backbone to help specific binding residues in recognizing base pairs correctly.

The logarithm of the free binding energy and the binding residues is shown in Table S2 (Supplementary data).

Three adenosine-binding residues were identified based on human cryptochrome DASH (chain X; PDB ID 2IJG) [ 31, 32], six phosphate-binding residues were identified based on photolyase-like domain of cryptochrome 1 (chain A; PDB ID 1U3C) [ 33], eleven flavin-binding residues were identified based on photolyase (chain A; PDB ID 1IQR) [ 34], and four were identified based on other protein templates.

Nine nicotinamide-binding residues were identified based on aldehyde dehydrogenase (chain A; PDB ID 3B4W), three phosphate-binding and eight adenosine-binding residues were identified based on 1-pyrroline-5-carboxylate dehydrogenase (chain A; PDB ID 2EHU), and three were identified based on other protein templates.

Five adenosine-binding residues were predicted based on putidaredoxin reductase (chain B; PDB ID 1Q1R) [ 36, 37], three adenosine-binding and nine flavin-binding residues based on D-amino acid oxidase (chain A; PDB ID 1C0I) [ 38], three phosphate-binding and five flavin-binding residues based on glycine oxidase (chain B; PDB ID 1NG3) [ 39], and five based on other protein templates.

Another way to find potential disorder-based binding sites is based on looking for residues in disordered regions that cannot form enough favorable intra-chain interactions to fold on their own, but which are likely to gain stabilizing energy by interacting with a globular protein partner.

The metal binding residues are not conserved.

It is based on the number of consecutive binding residues in the amino acid sequences.

The CPASS alignment is shown in Figure 2A and is based on maximizing the spatial orientation of similar residue types between the two ligand-binding sites.