{
  "annotation_id": "40f0c7eb-e996-4938-8c47-f139f6b81495",
  "date_created": "2026-03-02T18:01:28.597000Z",
  "date_modified": "2026-03-02T18:01:28.597000Z",
  "file_hash": "0d580e55dda750cef129e85e4697593fd9685d00ed51a1dff700bb037f189dc9",
  "private": false,
  "record": {
    "abstract": "The molecular mechanism of the solvent motion that is required to instigate\nthe protein structural relaxation above a critical hydration level or\ntransition temperature has yet to be determined. In this work we use\nquasi-elastic neutron scattering (QENS) and molecular dynamics simulation to\ninvestigate hydration water dynamics near a greatly simplified protein surface.\nWe consider the hydration water dynamics near the completely deuterated\nN-acetyl-leucine-methylamide (NALMA) solute, a hydrophobic amino acid side\nchain attached to a polar blocked polypeptide backbone, as a function of\nconcentration between 0.5M-2.0M, under ambient conditions. In this\nCommunication, we focus our results of hydration dynamics near a model protein\nsurface on the issue of how enzymatic activity is restored once a critical\nhydration level is reached, and provide a hypothesis for the molecular\nmechanism of the solvent motion that is required to trigger protein structural\nrelaxation when above the hydration transition.",
    "arxiv_id": "q-bio/0310013",
    "authors": [
      "Daniela Russo",
      "Greg Hura",
      "Teresa Head-Gordon"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "title": "Hydration Water Dynamics and Instigation of Protein Structural   Relaxation",
    "url": "https://arxiv.org/abs/q-bio/0310013"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "952ebd9d-cb95-48e4-9e40-d29bb2dbde16",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}