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Effects of adenosine diphosphate on the structure of myosin cross-bridges: An X-ray diffraction study on a single skinned frog muscle fibre
Author(s): Takemori S, Yamaguchi M, Yagi N
Source: JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY    Volume: 16    Issue: 6    Pages: 571-577    Published: DEC 1995  
Times Cited: 12     References: 24     
Abstract: Using a technique to obtain a detailed X-ray diffraction pattern from a single skinned frog muscle fibre, we studied the effects of ADP on the structure and arrangement of myosin heads. An imaging plate and a cooled-CCD X-ray detector were used to record the diffraction patterns. Addition of 1 mM ADP to a rigor fibre increased the intensity of the third-order meridional reflection of the myosin repeat by 50-85%. The intensity of the sixth-order meridional reflection also increased. After removing the ADP, these intensities decreased but did not return to the level before the ADP was added. No significant changes were observed in the intensities of the equatorial reflections and the actin layer-lines. These results suggest that, upon ADP binding, the conformation of a myosin head changes without detaching from actin. The structural change may involve a relative motion between domains of the myosin head by the closure of the cleft to which an ADP molecule binds.
Document Type: Article
Language: English
Reprint Address: Takemori, S (reprint author), JIKEI UNIV, SCH MED, DEPT PHYSIOL, MINATO KU, TOKYO 105, JAPAN
Addresses:
1. TOHOKU UNIV, SCH MED, DEPT PHARMACOL, AOBA KU, SENDAI, MIYAGI 98077 JAPAN
Publisher: CHAPMAN HALL LTD, 2-6 BOUNDARY ROW, LONDON, ENGLAND SE1 8HN
Subject Category: Cell Biology
IDS Number: TK558
ISSN: 0142-4319
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