dorsal/arxiv
View SchemaIntegrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank
| Authors | Chih-Yuan Tseng, Chun-Ping Yu, HC Lee |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0603033 |
| URL | https://arxiv.org/abs/q-bio/0603033 |
| DOI | 10.1007/s00249-009-0414-4 |
| License | http://arxiv.org/licenses/nonexclusive-distrib/1.0/ |
Abstract
In the template-assistance model, normal prion protein (PrPC), the pathogenic cause of prion diseases such as Creutzfeldt-Jakob (CJD) in human, Bovine Spongiform Encephalopathy (BSE) in cow, and scrapie in sheep, converts to infectious prion (PrPSc) through an autocatalytic process triggered by a transient interaction between PrPC and PrPSc. Conventional studies suggest the S1-H1-S2 region in PrPC to be the template of S1-S2 $\beta$-sheet in PrPSc, and the conformational conversion of PrPC into PrPSc may involve an unfolding of H1 in PrPC and its refolding into the $\beta$-sheet in PrPSc. Here we conduct a series of simulation experiments to test the idea of transient interaction of the template-assistance model. We find that the integrity of H1 in PrPC is vulnerable to a transient interaction that alters the native dihedral angles at residue Asn$^{143}$, which connects the S1 flank to H1, but not to interactions that alter the internal structure of the S1 flank, nor to those that alter the relative orientation between H1 and the S2 flank.
{
"annotation_id": "7c987c18-03d6-4511-8f11-0bf378d536e2",
"date_created": "2026-03-02T18:01:34.902000Z",
"date_modified": "2026-03-02T18:01:34.902000Z",
"file_hash": "edd5f65d48b347953cdc4e8f1dc4eea3e1cf360a8fc4766659e71179d0fe7677",
"private": false,
"record": {
"abstract": "In the template-assistance model, normal prion protein (PrPC), the pathogenic\ncause of prion diseases such as Creutzfeldt-Jakob (CJD) in human, Bovine\nSpongiform Encephalopathy (BSE) in cow, and scrapie in sheep, converts to\ninfectious prion (PrPSc) through an autocatalytic process triggered by a\ntransient interaction between PrPC and PrPSc. Conventional studies suggest the\nS1-H1-S2 region in PrPC to be the template of S1-S2 $\\beta$-sheet in PrPSc, and\nthe conformational conversion of PrPC into PrPSc may involve an unfolding of H1\nin PrPC and its refolding into the $\\beta$-sheet in PrPSc. Here we conduct a\nseries of simulation experiments to test the idea of transient interaction of\nthe template-assistance model. We find that the integrity of H1 in PrPC is\nvulnerable to a transient interaction that alters the native dihedral angles at\nresidue Asn$^{143}$, which connects the S1 flank to H1, but not to interactions\nthat alter the internal structure of the S1 flank, nor to those that alter the\nrelative orientation between H1 and the S2 flank.",
"arxiv_id": "q-bio/0603033",
"authors": [
"Chih-Yuan Tseng",
"Chun-Ping Yu",
"HC Lee"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1007/s00249-009-0414-4",
"license": "http://arxiv.org/licenses/nonexclusive-distrib/1.0/",
"title": "Integrity of H1 helix in prion protein revealed by molecular dynamic simulations to be especially vulnerable to changes in the relative orientation of H1 and its S1 flank",
"url": "https://arxiv.org/abs/q-bio/0603033"
},
"schema_id": "dorsal/arxiv",
"source": {
"execution_id": "5dc933a3-e4cd-4f66-a439-236247236f92",
"id": "arXiv Dataset IDs",
"type": "Model",
"variant": "snapshot-2026-03-01",
"version": "0.1.0"
},
"user_id": 1000002
}