Pathway Shifts and Thermal Softening in Temperature-Coupled Forced Unfolding of Spectrin Domains

Pathways of unfolding a protein depend in principle on the perturbation—whether it is temperature, denaturant, or even forced extension. Widely-shared, helical-bundle spectrin repeats are known to melt at temperatures as low as 40–45°C and are also known to unfold via multiple pathways as single mol...

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Bibliographic Details
Main Authors: Law, Richard, Liao, George, Harper, Sandy, Yang, Guoliang, Speicher, David W., Discher, Dennis E.
Format: Artigo
Language:Inglês
Published: Biophysical Society 2003
Subjects:
Proteins
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1303605/
https://ncbi.nlm.nih.gov/pubmed/14581229
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