3AGH: X-Ray Analysis Of Lysozyme In The Presence Of 200 Mm Arg

While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg-lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation-pi interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.
PDB ID: 3AGHDownload
MMDB ID: 89338
PDB Deposition Date: 2010/3/31
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 1.49  Å
Source Organism:
Similar Structures:
Biological Unit for 3AGH: monomeric; determined by author and by software (PISA)
Molecular Components in 3AGH
Label Count Molecule
Protein (1 molecule)
Lysozyme C(Gene symbol: LYZ)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB