Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy.
α-Tropomyosin (αTm) is the predominant tropomyosin isoform in adult human heart and constitutes a major component in Ca²+-regulated systolic contraction of cardiac muscle. We present here the first direct probe images of WT human cardiac αTm by atomic force microscopy, and quantify its mechanical fl...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3380901?pdf=render |
| _version_ | 1818381752183291904 |
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| author | Campion K P Loong Huan-Xiang Zhou P Bryant Chase |
| author_facet | Campion K P Loong Huan-Xiang Zhou P Bryant Chase |
| author_sort | Campion K P Loong |
| collection | DOAJ |
| description | α-Tropomyosin (αTm) is the predominant tropomyosin isoform in adult human heart and constitutes a major component in Ca²+-regulated systolic contraction of cardiac muscle. We present here the first direct probe images of WT human cardiac αTm by atomic force microscopy, and quantify its mechanical flexibility with three independent analysis methods. Single molecules of bacterially-expressed human cardiac αTm were imaged on poly-lysine coated mica and their contours were analyzed. Analysis of tangent-angle (θ(s)) correlation along molecular contours, second moment of tangent angles (<θ²(s)>), and end-to-end length (L(e-e)) distributions respectively yielded values of persistence length (L(p)) of 41-46 nm, 40-45 nm, and 42-52 nm, corresponding to 1-1.3 molecular contour lengths (L(c)). We also demonstrate that a sufficiently large population, with at least 100 molecules, is required for a reliable L(p) measurement of αTm in single molecule studies. Our estimate that L(p) for αTm is only slightly longer than L(c) is consistent with a previous study showing there is little spread of cooperative activation into near-neighbor regulatory units of cardiac thin filaments. The L(p) determined here for human cardiac αTm perhaps represents an evolutionarily tuned optimum between Ca²+ sensitivity and cooperativity in cardiac thin filaments and likely constitutes an essential parameter for normal function in the human heart. |
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| id | doaj.art-8c160f0f0a0a49f295218cc63c21bcb0 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T02:39:34Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
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| series | PLoS ONE |
| spelling | doaj.art-8c160f0f0a0a49f295218cc63c21bcb02022-12-21T23:20:02ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0176e3967610.1371/journal.pone.0039676Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy.Campion K P LoongHuan-Xiang ZhouP Bryant Chaseα-Tropomyosin (αTm) is the predominant tropomyosin isoform in adult human heart and constitutes a major component in Ca²+-regulated systolic contraction of cardiac muscle. We present here the first direct probe images of WT human cardiac αTm by atomic force microscopy, and quantify its mechanical flexibility with three independent analysis methods. Single molecules of bacterially-expressed human cardiac αTm were imaged on poly-lysine coated mica and their contours were analyzed. Analysis of tangent-angle (θ(s)) correlation along molecular contours, second moment of tangent angles (<θ²(s)>), and end-to-end length (L(e-e)) distributions respectively yielded values of persistence length (L(p)) of 41-46 nm, 40-45 nm, and 42-52 nm, corresponding to 1-1.3 molecular contour lengths (L(c)). We also demonstrate that a sufficiently large population, with at least 100 molecules, is required for a reliable L(p) measurement of αTm in single molecule studies. Our estimate that L(p) for αTm is only slightly longer than L(c) is consistent with a previous study showing there is little spread of cooperative activation into near-neighbor regulatory units of cardiac thin filaments. The L(p) determined here for human cardiac αTm perhaps represents an evolutionarily tuned optimum between Ca²+ sensitivity and cooperativity in cardiac thin filaments and likely constitutes an essential parameter for normal function in the human heart.http://europepmc.org/articles/PMC3380901?pdf=render |
| spellingShingle | Campion K P Loong Huan-Xiang Zhou P Bryant Chase Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. PLoS ONE |
| title | Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. |
| title_full | Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. |
| title_fullStr | Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. |
| title_full_unstemmed | Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. |
| title_short | Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy. |
| title_sort | persistence length of human cardiac α tropomyosin measured by single molecule direct probe microscopy |
| url | http://europepmc.org/articles/PMC3380901?pdf=render |
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