Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 25, Pages 10459-10464Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0704073104
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Funding
- NCI NIH HHS [R01-CA116583-01, R01 CA116583] Funding Source: Medline
- NIA NIH HHS [1-R21-AG026650, R21 AG026650] Funding Source: Medline
- NIBIB NIH HHS [P41 EB001976] Funding Source: Medline
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The spectra of equilibrium chain conformation fluctuations of apomyoglobin (apoMb) as a function of folding, from the acid-denatured state at pH 2.6 through the stable molten globule state pH approximate to 4.1 to the folded state at pH 6.3, are reported, as measured by fluorescence correlation spectroscopy. The conformational fluctuations, which are detected by quenching of an N-terminal fluorescent label by contact with various amino acids, can be represented by superpositions of decaying exponentials with time scales ranging from approximate to 3 to approximate to 200 mu s. Both the time scales and amplitudes of the fluctuations increase with the degree of acid denaturation, with principal shifts associated with the transition across the molten globule state. Measurements of the diffusion of apoMb confirm theoretical values showing a approximate to 40% increase in the hydrodynamic radius upon acid denaturation. This study uses the model protein apoMb to illustrate the complex scope of folding-associated structural dynamics.
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