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apomyoglobin

 
National Institutes of Health

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Highly Cited
2004
Highly Cited
2004
The conformational propensities of unfolded states of apomyoglobin have been investigated by measurement of residual dipolar… Expand
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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… Expand
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Highly Cited
1997
Highly Cited
1997
We show here that limited proteolysis can probe the structural and dynamic differences between the holo and apo form of horse… Expand
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Highly Cited
1996
Highly Cited
1996
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms… Expand
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1994
1994
A recently developed approach to calculate the pH dependence of protein stability from three-dimensional structure information is… Expand
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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… Expand
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Highly Cited
1990
Highly Cited
1990
To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of… Expand
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1988
1988
Sperm whale apomyoglobin has been studied thermodynamically in solutions with different pH and temperature by scanning… Expand
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Highly Cited
1967
Highly Cited
1967
The protein sequenator is an instrument for the automatic determination of amino acid sequences in proteins and peptides. It… Expand
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Highly Cited
1965
Highly Cited
1965
1-Anilino-8-naphthalene sulfonate binds stoichiometrically to a specific site on apomyoglobin and apohemoglobin. One mole of ANS… Expand
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