{"paper":{"title":"Characterizing the folding core of the cyclophilin A - cyclosporin A complex II: improving folding core predictions by including mobility","license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","headline":"","cross_cats":[],"primary_cat":"q-bio.BM","authors_text":"J. W. Heal, R. A. R\\\"omer, R. B. Freedman, S. A. Wells","submitted_at":"2014-07-16T19:37:16Z","abstract_excerpt":"Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino acids which make up the folding core include hydrogen-deuterium exchange and $\\Phi$-value analysis and can be expensive and time consuming. As such there is a desire to improve upon existing methods for determining protein folding cores theoretically. Here, we use a combined method of rigidity analysis alongside coarse-grained simulations of protein motion in order to improve folding core predictions for unbound CypA and for the CypA-CsA com"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"1407.4440","kind":"arxiv","version":1},"verdict":{"id":null,"model_set":{},"created_at":null,"strongest_claim":"","one_line_summary":"","pipeline_version":null,"weakest_assumption":"","pith_extraction_headline":""},"references":{"count":0,"sample":[],"resolved_work":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57","internal_anchors":0},"formal_canon":{"evidence_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"author_claims":{"count":0,"strong_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"builder_version":"pith-number-builder-2026-05-17-v1"}