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Полная запись метаданных
Поле DC | Значение | Язык |
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dc.contributor.author | Blyakhman, F. | en |
dc.contributor.author | Tourovskaya, A. | en |
dc.contributor.author | Pollack, G. H. | en |
dc.date.accessioned | 2022-05-12T08:21:09Z | - |
dc.date.available | 2022-05-12T08:21:09Z | - |
dc.date.issued | 2001 | - |
dc.identifier.citation | Blyakhman F. Quantal Sarcomere-length Changes in Relaxed Single Myofibrils / F. Blyakhman, A. Tourovskaya, G. H. Pollack // Biophysical Journal. — 2001. — Vol. 81. — Iss. 2. — P. 1093-1100. | en |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.other | All Open Access, Bronze, Green | 3 |
dc.identifier.uri | http://elar.urfu.ru/handle/10995/111714 | - |
dc.description.abstract | We carried out experiments on single isolated myofibrils in which thin filaments had been functionally removed, leaving the connecting (titin) filaments as the sole agent taking up the length change. With technical advances that gave sub-nanometer detectability we examined the time course of single sarcomere-length change when the myofibril was ramp-released or ramp-stretched by a motor. The sarcomere-length change was stepwise. Step sizes followed a consistent pattern: the smallest was ∼2.3 nm, and others were integer multiples of that value. The ∼2.3-nm step quantum is the smallest consistent biomechanical event ever demonstrated. Although the length change must involve the connecting filament, the size of the quantum is an order of magnitude smaller than anticipated from folding of Ig- or fibronectin-like domains, implying either that folding occurs in sub-domain units or that other mechanisms are involved. | en |
dc.format.mimetype | application/pdf | en |
dc.language.iso | en | en |
dc.publisher | Biophysical Society | en1 |
dc.publisher | Elsevier BV | en |
dc.rights | info:eu-repo/semantics/openAccess | en |
dc.source | Biophys. J. | 2 |
dc.source | Biophysical Journal | en |
dc.subject | CONNECTIN | en |
dc.subject | FIBRONECTIN | en |
dc.subject | ANIMAL CELL | en |
dc.subject | ARTICLE | en |
dc.subject | MUSCLE FIBRIL | en |
dc.subject | NONHUMAN | en |
dc.subject | PROTEIN DOMAIN | en |
dc.subject | PROTEIN FOLDING | en |
dc.subject | QUANTUM MECHANICS | en |
dc.subject | RELAXATION TIME | en |
dc.subject | SARCOMERE | en |
dc.subject | SARCOMERE LENGTH | en |
dc.subject | ANIMALIA | en |
dc.title | Quantal Sarcomere-length Changes in Relaxed Single Myofibrils | en |
dc.type | Article | en |
dc.type | info:eu-repo/semantics/article | en |
dc.type | info:eu-repo/semantics/publishedVersion | en |
dc.identifier.scopus | 0034906672 | - |
local.contributor.employee | Blyakhman, F., Department of Bioengineering, University of Washington, Seattle, WA 98195, United States, Department of Physics, Ural State University, Ekaterinburg, Russian Federation; Tourovskaya, A., Department of Bioengineering, University of Washington, Seattle, WA 98195, United States; Pollack, G.H., Department of Bioengineering, University of Washington, Seattle, WA 98195, United States, University of Washington, Department of Bioengineering, Box 357962, Seattle, WA 98195, United States | en |
local.description.firstpage | 1093 | - |
local.description.lastpage | 1100 | - |
local.issue | 2 | - |
local.volume | 81 | - |
local.contributor.department | Department of Bioengineering, University of Washington, Seattle, WA 98195, United States; Department of Physics, Ural State University, Ekaterinburg, Russian Federation; University of Washington, Department of Bioengineering, Box 357962, Seattle, WA 98195, United States | en |
local.identifier.eid | 2-s2.0-0034906672 | - |
local.identifier.pmid | 11463650 | - |
Располагается в коллекциях: | Научные публикации ученых УрФУ, проиндексированные в SCOPUS и WoS CC |
Файлы этого ресурса:
Файл | Описание | Размер | Формат | |
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2-s2.0-0034906672.pdf | 261,01 kB | Adobe PDF | Просмотреть/Открыть |
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