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Collective motions ...
Collective motions and structural self-organisation along the myoglobin folding pathway
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- Peng, Xubiao (author)
- Uppsala universitet,Teoretisk fysik
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- Sieradzan, Adam K. (author)
- Uppsala universitet,Teoretisk fysik,Faculty of Chemistry, University of Gdansk
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- Scheraga, Harold A. (author)
- Baker Laboratory of Chemistry and Chemical Biology, Cornell University
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- Niemi, Antti (author)
- Uppsala universitet,Teoretisk fysik
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(creator_code:org_t)
- English.
- Related links:
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https://urn.kb.se/re...
Abstract
Subject headings
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- We develop a highly predictive energy function to describe the low temperature crystallographic structure of myoglobin with sub-\AA ngstr\"om precision. We use the energy function to investigate the way how myoglobin folds.For this we employ the Glauber protocol, with a variable ambient temperature. We first increase the temperature so that the structure unfolds into a random coil. We then lower thetemperature back to its original value, and monitor how the myoglobin folds towards its native state.We find that the folding proceeds by $\alpha$-helix nucleation, and that the ordering of helix formation parallels experimental observations. There is also a molten globule folding intermediate, with a radius of gyration that matches the experimentally measured value. We estimate the relative folding times between a random chain and molten globule, and between molten globule and the native state, and we find that the ratio is consistentwith the experimentally measured values. We also propose a number of novel experimental characteristics that could be measured in future experiments.
Subject headings
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
Publication and Content Type
- vet (subject category)
- ovr (subject category)
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