{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,6]],"date-time":"2026-02-06T23:55:28Z","timestamp":1770422128485,"version":"3.49.0"},"reference-count":15,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2001,11,12]],"date-time":"2001-11-12T00:00:00Z","timestamp":1005523200000},"content-version":"vor","delay-in-days":6503,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1984,1,23]]},"abstract":"<jats:p>Hemoglobin Chemilly (\u03b1<jats:sub>2<\/jats:sub>\u03b2<jats:sub>2<\/jats:sub> 99(G1)Asp\u2192Val), a high oxygen affinity variant, was uncovered in the red blood cells of a polycythemic patient who reported to the hospital concerning periodic headaches. We describe the molecular abnormality and functional studies of this new abnormal Hb. \u03b2 99(G1)Asp, an invariant residue of hemoglobin, is considered a key amino acid for conformational changes between the R\u21c6T quaternary structures responsible for the allosteric behavior of hemoglobin. Hb Chemilly exhibits a high 0<jats:sub>2<\/jats:sub> affinity, very low cooperativity and reduced Bohr effect. Its functional abnormalities are compared to the 5 other Hb variants at site \u03b2 99(G1) described up to now of the 7 single base substitutions predictable from the genetic code.<\/jats:p>","DOI":"10.1016\/0014-5793(84)80034-4","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T09:35:43Z","timestamp":1027589743000},"page":"8-12","source":"Crossref","is-referenced-by-count":25,"title":["A new hemoglobin variant altering the \u03b1<sub>1<\/sub>\u03b2<sub>2<\/sub> contact: Hb Chemilly \u03b1<sub>2<\/sub>\u03b2<sub>2<\/sub> 99(G1)Asp\u2192Val"],"prefix":"10.1002","volume":"166","author":[{"given":"J.","family":"Rochette","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C.","family":"Poyart","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B.","family":"Varet","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.","family":"Wajcman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2001,11,12]]},"reference":[{"key":"e_1_2_1_2_1","volume-title":"Haemoglobin and Myoglobin","author":"Fermi G.","year":"1981"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(79)90277-8"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI105674"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.7326\/0003-4819-69-4-769"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V31.5.623.623"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2141.1977.tb00575.x"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2795(81)90018-0"},{"key":"e_1_2_1_9_1","first-page":"760","volume":"13","author":"Korubin V.","year":"1972","journal-title":"J. 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