HEWL Crystals Soaked in Guanidine Hydrochloride for Time-Dependent Binding Analysis

X-ray structures reveal guanidinium ions preferentially hydrogen bonding with backbone carbonyl oxygen atoms, replacing water molecules in hen egg-white lysozyme crystals. The number of water molecules in the protein's first solvent shell decreased from 152 to 115 after soaking in 2.5M GuHCl. This dataset, from Universität Hamburg, investigates the structural effects of GuHCl binding, linking it to destabilization mechanisms seen in amyloidogenic variants.

Use Cases

• Modeling protein-solvent interactions based on the described displacement of water molecules by guanidinium ions.
• Analyzing hydrogen bond weakening in main chain atoms as a mechanism for denaturant potency.
• Studying domain destabilization, specifically in the β-domain, due to loss of hydrogen bonds involving Asn 59.
• Investigating anti-amyloidogenic compound design based on the described structural loss identical to human lysozyme variants.

Strengths

• Describes a specific experimental setup with 2.5M GuHCl concentration and 20-minute soaking times.
• Quantifies a structural change: water molecules in the first solvent shell decreased from 152 to 115.
• Identifies a precise molecular interaction: guanidinium ions preferentially hydrogen bond with backbone carbonyl oxygen atoms.

Limitations

• Row count and column-level documentation are absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

Universität Hamburg

Collection Method

X-ray crystallography of hen egg-white lysozyme crystals soaked in GuHCl solutions.