apomyoglobin

 
National Institutes of Health

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Topic mentions per year

1962-2017
0102019622017

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2001
2001
Apomyoglobin forms a denatured state under low-salt conditions at pH 2.3. The conformational propensities and polypeptide… (More)
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Highly Cited
1998
Highly Cited
1998
The structure and dynamics of two partially folded states of apomyoglobin have been characterized at equilibrium using multi… (More)
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1998
1998
The pH 4 folding intermediate of apomyoglobin exists in two forms (Ia, Ib) at equilibrium. Their ratio depends on pH, urea… (More)
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1997
1997
We report the fast relaxation dynamics of "native" apomyoglobin (pH 5.3) following a 10-ns, laser-induced temperature jump. The… (More)
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1997
1997
We show here that limited proteolysis can probe the structural and dynamic differences between the holo and apo form of horse… (More)
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1996
1996
Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural information on isotopically labeled… (More)
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1996
1996
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms… (More)
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1994
1994
It has been shown that a compact, partly unfolded state of apomyoglobin, which is obtained in acidic solutions, had a heat… (More)
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Highly Cited
1993
Highly Cited
1993
Hydrogen exchange pulse labeling and stopped-flow circular dichroism were used to establish that the structure of the earliest… (More)
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1990
Highly Cited
1990
To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of… (More)
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