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apomyoglobin

National Institutes of Health

Papers overview

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Highly Cited
2003
Highly Cited
2003
Very little is known about how protein structure evolves during the polypeptide chain elongation that accompanies cotranslational… 
Highly Cited
1999
Highly Cited
1999
The hydration of nonnative states is central to protein folding and stability but has been probed mainly by indirect methods… 
Highly Cited
1994
Highly Cited
1994
A recently developed approach to calculate the pH dependence of protein stability from three-dimensional structure information is… 
Highly Cited
1994
Highly Cited
1994
It has been shown that a compact, partly unfolded state of apomyoglobin, which is obtained in acidic solutions, had a heat… 
Highly Cited
1994
Highly Cited
1994
Apomyoglobin adopts a partly folded intermediate conformation (I), sometimes referred to as a molten globule intermediate, near… 
Highly Cited
1994
Highly Cited
1994
Apomyoglobin, myoglobin lacking the haem group, is a natural intermediate in biosynthesis of myoglobin, and has some structural… 
Highly Cited
1992
Highly Cited
1992
Proton NMR spectroscopy was applied to myoglobin in the ferric, water-liganded form (metMbH2O) and the apo form (apoMb) to probe… 
Highly Cited
1966
Highly Cited
1966
1. No ferrihaem was detected in the precipitate formed by metmyoglobin with an antiserum to apomyoglobin and the extinction at…