Stable single ?-helices are constant force springs in proteins.
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ABSTRACT:
SUBMITTER: Wolny M
PROVIDER: S-EPMC4183817 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Publications
Stable single α-helices are constant force springs in proteins.
Wolny Marcin M Batchelor Matthew M Knight Peter J PJ Paci Emanuele E Dougan Lorna L Peckham Michelle M
The Journal of biological chemistry 20140813 40
Single α-helix (SAH) domains are rich in charged residues (Arg, Lys, and Glu) and stable in solution over a wide range of pH and salt concentrations. They are found in many different proteins where they bridge two functional domains. To test the idea that their high stability might enable these proteins to resist unfolding along their length, the properties and unfolding behavior of the predicted SAH domain from myosin-10 were characterized. The expressed and purified SAH domain was highly helic ...[more]
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