{"paper":{"title":"Modulation of N- to C-terminal interactions enhances protein stability","license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","headline":"","cross_cats":[],"primary_cat":"q-bio.BM","authors_text":"A. Bhardwaj, K. Kumar, P. Mahanta, S. Ramakumar, V.S. Reddy","submitted_at":"2015-01-12T16:42:29Z","abstract_excerpt":"Although, several factors have been attributed to thermostability, the stabilization strategies used by proteins are still enigmatic. Studies on recombinant xylanase which has the ubiquitous (\\b{eta}/{\\alpha})8 TIM (Triosephosphate isomerase) barrel fold showed that, just a single extreme N-terminus mutation (V1L) markedly enhanced the thermostability by 5 {\\deg}C without loss of catalytic activity whereas another mutation, V1A at the same position decreased the stability by 2 {\\deg}C. Based on computational analysis of their crystal structures including residue interaction network, we establi"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"1501.02709","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"}