1                              The assembly of Scapharca dimeric hemoglobin as a function of ligation h

2  of structural changes in single crystals of Scapharca dimeric hemoglobin as they proceed in real tim

3 of the most remarkable structural aspects of Scapharca dimeric hemoglobin is the disruption of a very

4 ntral role in the cooperative functioning of Scapharca dimeric hemoglobin, has been mutated to leucin

5 he most dramatic ligand-linked transition in Scapharca dimeric hemoglobin, with its packing in the he

6 ernary constraint underlies cooperativity in Scapharca dimeric hemoglobin.

7 parallel pathways for communication exist in Scapharca dimeric hemoglobin.

8                    The dimeric hemoglobin of Scapharca (HbI), which is composed of subunits with the

9              These observations suggest that Scapharca hemoglobin has a unique heme structure that un

10                                    Wild-type Scapharca hemoglobin is strongly sensitive to osmotic co

11 an hemoglobin, raises the oxygen affinity of Scapharca hemoglobin regardless of whether the solute is

12       These findings suggest that in dimeric Scapharca hemoglobin the photoproduct has not relaxed af

13           The ferric form of the homodimeric Scapharca hemoglobin undergoes a pH-dependent spin trans

14 e kinetics of the R-to-T transition in deoxy Scapharca hemoglobin.

15 igated in deoxy and photodissociated dimeric Scapharca hemoglobin.

16 dimeric hemoglobin (HbI) from the blood clam Scapharca inaequivalvis is mediated primarily by tertiar

17 n the dimeric hemoglobin from the blood clam Scapharca inaequivalvis results primarily from tertiary,

18 ategy to the homodimeric hemoglobin HbI from Scapharca inaequivalvis.

19 mmunication in the homodimeric hemoglobin of Scapharca inaequivalvis.