Funneled angle landscapes for helical proteins
We use crystallographic data for four helical iron proteins (cytochrome c-b₅₆₂, cytochrome c′, sperm whale myoglobin, human cytoglobin) to calculate radial and angular signatures as each unfolds from the native state stepwise though four unfolded states. From these data we construct an angle...
Published in: | Journal of Inorganic Biochemistry |
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Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
Elsevier
2020
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Subjects: | |
Online Access: | https://doi.org/10.1016/j.jinorgbio.2020.111091 https://www.ncbi.nlm.nih.gov/pmc/PMC7453651 |
Summary: | We use crystallographic data for four helical iron proteins (cytochrome c-b₅₆₂, cytochrome c′, sperm whale myoglobin, human cytoglobin) to calculate radial and angular signatures as each unfolds from the native state stepwise though four unfolded states. From these data we construct an angle phase diagram to display the evolution of each protein from its native state; and, in turn, the phase diagram is used to construct a funneled angle landscape for comparison with the topography of its folding energy landscape. We quantify the departure of individual helical and turning regions from the areal, angular profile of corresponding regions of the native state. This procedure allows us to identify the similarities and differences among individual helical and turning regions in the early stages of unfolding of the four helical heme proteins. © 2020 Published by Elsevier Inc. Received 4 January 2020, Revised 14 April 2020, Accepted 16 April 2020, Available online 11 May 2020. We thank Devarajan (Dave) Thirumalai for very helpful comments. Work at Caltech was supported by the NIH (DK019038) and the Arnold and Mabel Beckman Foundation. Support at Pomona College was provided by the Howard Hughes Medical Institute Research Program and a Sontag Research Fellowship Award. The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Accepted Version - 1-s2.0-S0162013420301197-main.pdf Accepted Version - nihms-1601242.pdf Supplemental Material - 1-s2.0-S0162013420301197-mmc1.docx |
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