{"record":{"author":{"account_ref":null,"orcid":null},"builds_on":[],"content_schema":"pubphys.content.topic/1","content_sha256":"33d190700b5a9a71f96a9de7e736c0058e0511e3c954a8f2d1a06e26db5dc045","created":"2026-10-03T07:17:50Z","files":[],"origin":{"assisted_by":[],"kind":"seed"},"parents":[],"salt":"889870968828b813c9e05f1babde1e671aa12271956eda5b25422abc23075bad","schema":"pubphys.record/2","site":"pubphys.com","target":null,"type":"topic"},"content":{"external_id":"bio.protein-folding","field":"bio","n":"1","review_cite":"Jose Nelson Onuchic, Peter G. Wolynes, Theory of protein folding, Current Opinion in Structural Biology, 2004","review_link":"https://doi.org/10.1016/j.sbi.2004.01.009","review_verified":"true","summary":"A protein is a chain of amino acids that folds itself into a precise 3D shape, often in well under a second. Computers now predict the final shape well, but not how fast the chain folds, by which route, or why it sometimes misfolds into clumps.","title":"Protein folding kinetics and energy landscapes","topic_ref":null,"why":"Folding rates and misfolding decide whether proteins work or form the toxic aggregates seen in Alzheimer's and Parkinson's diseases."},"attested":{"attestation":{"batch":null,"client_id":null,"id_token_sha256":null,"kind":"platform"},"record_hash":"d70805bb63f25bf8902aa9ee3d70d8c036572d9638addfbea7d1b841f5ab7b17","schema":"pubphys.attested/1"},"envelope":{"attested_hash":"0a50f9bb40e2eda5ce6c9ece978881a96affa851efe79bb5a0ae6857df0ae291","platform_signature":{"key_id":"c6afc19b31429869751f06879c75cd64ea92654423d15b44be775bf1310a60da","sig":"kCJDzUSU7h_ajo5k5QllQX2v-kNcfB6y1aV-7S3HSVXuYhkyHbBuywHOm2jrpsM3qXLLYqvYy8cEhrxDRI0YAQ"},"schema":"pubphys.envelope/1"},"record_hash":"d70805bb63f25bf8902aa9ee3d70d8c036572d9638addfbea7d1b841f5ab7b17","leaf_index":100}