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Normal and abnormal protein subunit interactions in hemoglobins.
Manning JM, Dumoulin A, Li X, Manning LR. Manning JM, et al. Among authors: dumoulin a. J Biol Chem. 1998 Jul 31;273(31):19359-62. doi: 10.1074/jbc.273.31.19359. J Biol Chem. 1998. PMID: 9677349 Free article. Review. No abstract available.
The N-terminal sequence affects distant helix interactions in hemoglobin. Implications for mutant proteins from studies on recombinant hemoglobin felix.
Dumoulin A, Padovan JC, Manning LR, Popowicz A, Winslow RM, Chait BT, Manning JM. Dumoulin A, et al. J Biol Chem. 1998 Dec 25;273(52):35032-8. doi: 10.1074/jbc.273.52.35032. J Biol Chem. 1998. PMID: 9857036 Free article.
Even though Hb Felix contains the HbA amino acids at its tetramer-dimer interface, which is located at a distance from the substitution sites, its interface properties resemble those of HbF. Therefore, the N-terminal sequence and not just those amino acids directly involve …
Even though Hb Felix contains the HbA amino acids at its tetramer-dimer interface, which is located at a distance from the substituti …
141 results