PMC:2724026 / 27159-27585 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2724026","sourcedb":"PMC","sourceid":"2724026","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2724026","text":"Although FADD DD and TNfn3 have similar stabilities, and appear to have similar folding mechanisms, FADD DD folds significantly faster than TNfn3 (∼ 1000 s- 1 compared to 6 s- 1). This is not unexpected; FADD DD is an all alpha-helical protein with a significantly lower relative contact order than the all-beta TNfn3, and it has been shown that proteins with low contact orders generally have higher folding rate constants.44","tracks":[{"project":"2_test","denotations":[{"id":"19362094-9545386-62520539","span":{"begin":424,"end":426},"obj":"9545386"}],"attributes":[{"subj":"19362094-9545386-62520539","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#9493ec","default":true}]}]}}