Kinetics of conformation change of sperm-whale myoglobin. I. Folding and unfolding of metmyoglobin following pH jump

Biochemistry ◽  
1972 ◽  
Vol 11 (10) ◽  
pp. 1836-1841 ◽  
Author(s):  
Linus L. Shen ◽  
Jan Hermans
Keyword(s):  
Sperm Whale ◽  
Conformation Change ◽  
Ph Jump ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin

scholarly journals Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins

1987 ◽  
Vol 243 (1) ◽  
pp. 205-210 ◽  
Author(s):  
H S Aojula ◽  
M T Wilson ◽  
I E G Morrison
Keyword(s):  
Ligand Binding ◽  
Kinetic Parameters ◽  
Sperm Whale ◽  
Binding Kinetics ◽  
Orientational Disorder ◽  
Binding Properties ◽  
Functional Consequences ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin ◽  
O2 Dissociation

Ligand-binding kinetics of native and reconstituted sperm-whale myoglobin were studied in relation to haem orientational disorder by rapid kinetic methods. In addition, native yellow-fin-tuna myoglobin with significant amount of haem disorder was also used. The O2 dissociation and association rates were found for the proteins with different degrees of haem disorder, and these results suggest that the isomers are characterized by almost identical kinetic parameters. Rates of CO recombination after photolysis were also identical for the two orientational isomers. The results clearly indicate that the rotation of the haem about the alpha-gamma meso axis has little or no effect on the ligand-binding properties of these myoglobins.

scholarly journals 1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin

1988 ◽  
Vol 250 (3) ◽  
pp. 853-858 ◽  
Author(s):  
H S Aojula ◽  
M T Wilson ◽  
G R Moore ◽  
D J Williamson
Keyword(s):  
Sperm Whale ◽  
Orientational Disorder ◽  
Human Haemoglobin ◽  
Minor Isomer ◽  
Alternative Method ◽  
Freeze Dried ◽  
Ph Jump ◽  
Sperm Whale Myoglobin ◽  
Soret Region

1H-n.m.r. and c.d. studies on sperm-whale myoglobin show that the c.d. signal in the Soret region is inversely and linearly related to the proportion of minor isomer present. An alternative method, ‘pH jump’, is described for inducing orientational disorder in sperm-whale myoglobin without recourse to reconstitution. 1H-n.m.r. studies on human haemoglobin A indicate little heterogeneity in freshly isolated haemoglobin A, but the effect is enhanced in freeze-dried Sigma haemoglobin A.

scholarly journals The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin.

1990 ◽  
Vol 265 (6) ◽  
pp. 3168-3176 ◽  
Author(s):  
R J Rohlfs ◽  
A J Mathews ◽  
T E Carver ◽  
J S Olson ◽  
B A Springer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ligand Binding ◽  
Amino Acid Substitution ◽  
Sperm Whale ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin
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