ArticleBiophysical journal2001
Stability and folding rates of domains spanning the large A-band super-repeat of titin.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Pairwise sequence similarity mapping with PaSiMap: Reclassification of immunoglobulin domains from titin as case study.Computational and structural biotechnology journal · 2022Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- When signalling goes wrong: pathogenic variants in structural and signalling proteins causing cardiomyopathies.Journal of muscle research and cell motility · 2017Review
- Article
- Two immunoglobulin tandem proteins with a linking β-strand reveal unexpected differences in cooperativity and folding pathways.Journal of molecular biology · 2012Article
- Muscle giants: molecular scaffolds in sarcomerogenesis.Physiological reviews · 2009Review
- Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Complex folding kinetics of a multidomain protein.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is a very large (>3 MDa) protein found in striated muscle where it is believed to participate in myogenesis and passive tension. A prominent feature in the A-band portion of titin is the presence of an 11-domain super-repeat of immunoglobulin superfamily and fibronectin-type-III-like domains. Seven overlapping constructs from human cardiac titin, each consisting of two or three domains and together spanning the entire 11-domain super-repeat, have been expressed in Escherichia coli. Fluorescence unfolding experiments and circular dichroism spectroscopy have been used to measure folding stabilities for each of the constructs and to assign unfolding rates for each super-repeat domain. Immunoglobulin superfamily domains were found to fold correctly only in the presence of their C-terminal fibronectin type II domain, suggesting close and possibly rigid association between these units. The domain stabilities, which range from 8.6 to 42 kJ mol(-1) under physiological conditions, correlate with previously reported mechanical forces required to unfold titin domains. Individual domains vary greatly in their rates of unfolding, with a range of unfolding rate constants between 2.6 x 10(-6) and 1.2 s(-1). This variation in folding behavior is likely to be an important determinant in ensuring independent folding of domains in multi-domain proteins such as titin.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.