References
- Patrinos GP, Giardine B, Riemer C, et al. Improvements in the HbVar database of human hemoglobin variants and thalassemia mutations for population and sequence variation studies. Nucleic Acids Res. 2004;32(Database issue):D537–D541 (http://globin.cse.psu.edu/)
- Zimmerman SS, Scheraga HA. Influence of local interactions on protein structure. I. Conformational energy studies of N-Acetyl-N’-Methylamides of Pro-X and X-Pro dipeptides. Biopolymers. 1977;16(4):811–843
- Piela L, Nemethy G, Scheraga HA. Proline-induced constraints in α-helices. Biopolymers. 1987;26(9):1587–1600
- Tan AS, Quah TC, Low PS, Chong SS. A rapid and reliable 7-deletion multiplex polymerase chain reaction assay for α-thalassemia. Blood. 2001;98(1):250–251
- Barlow DJ, Thornton JM. Helix geometry in proteins. J Mol Biol. 1988;201(3):601–619
- Beuzard Y, Basset P, Braconnier F, et al. Hemoglobin Saki α2β214Leu → Pro (A11) structure and function. Biochim Biophys Acta. 1975;393(1):182–187
- Nakatsuji T, Miwa S, Ohba Y, et al. A new unstable hemoglobin, Hb Yokohama β31(B13)Leu → Pro, causing hemolytic anemia. Hemoglobin. 1981;5(7–8):667–678
- Milner PF, Corley CC, Pomeroy WL, et al. Thalassemia intermedia caused by heterozygosity for both β-thalassemia and Hemoglobin Saki [β14(A11)Leu → Pro]. Am J Hematol. 1976;1(3):283–292