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处于尸僵状态的紧张肌肉纤维的X射线衍射。

X-ray diffraction of strained muscle fibers in rigor.

作者信息

Naylor G R, Podolsky R J

出版信息

Proc Natl Acad Sci U S A. 1981 Sep;78(9):5559-63. doi: 10.1073/pnas.78.9.5559.

Abstract

The effect of strain on the equatorial x-ray diffraction pattern of glycerinated rabbit psoas fibers was studied in the rigor (ATP free) state. Strains between 30 and 100 A per half sarcomere, measured directly by laser diffraction, did not change the intensity ratio, (10)/ . (11). Because the intensity ratio depends on the distribution of mass within the myofilament lattice, the negative result indicates that strain does not change the angle of attachment of the subfragment 1 (S1) moiety of the myosin molecule to the actin filament. The effect of strain on the ordering of the actin filaments also was considered and judged to be negligible.

摘要

在僵直(无ATP)状态下,研究了应变对甘油处理的兔腰大肌纤维赤道X射线衍射图谱的影响。通过激光衍射直接测量,每半个肌节30至100埃之间的应变并未改变强度比(10)/.(11)。由于强度比取决于肌丝晶格内的质量分布,这一阴性结果表明应变不会改变肌球蛋白分子的亚片段1(S1)部分与肌动蛋白丝的附着角度。还考虑了应变对肌动蛋白丝有序排列的影响,并判断其可忽略不计。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79c6/348786/cfe0be319c76/pnas00660-0325-a.jpg

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