The conformation of myosin head domains in rigor muscle determined by X-ray interference

TY - JOUR

T1 - The conformation of myosin head domains in rigor muscle determined by X-ray interference

AU - Reconditi, M

AU - Koubassova, N

AU - Linari, M

AU - Dobbie, I

AU - Narayanan, T

AU - Diat, O

AU - Piazzesi, G

AU - Lombardi, V

AU - Irving, M

PY - 2003/8/1

Y1 - 2003/8/1

N2 - In the absence of adenosine triphosphate, the head domains of myosin cross-bridges in muscle bind to actin filaments in a rigor conformation that is expected to mimic that following the working stroke during active contraction. We used x-ray interference between the two head arrays in opposite halves of each myosin filament to determine the rigor head conformation in single fibers from frog skeletal muscle. During isometric contraction (force T-0), the interference effect splits the M3 x-ray reflection from the axial repeat of the heads into two peaks with relative intensity (higher angle/lower angle peak) 0.76. In demembranated fibers in rigor at low force (

AB - In the absence of adenosine triphosphate, the head domains of myosin cross-bridges in muscle bind to actin filaments in a rigor conformation that is expected to mimic that following the working stroke during active contraction. We used x-ray interference between the two head arrays in opposite halves of each myosin filament to determine the rigor head conformation in single fibers from frog skeletal muscle. During isometric contraction (force T-0), the interference effect splits the M3 x-ray reflection from the axial repeat of the heads into two peaks with relative intensity (higher angle/lower angle peak) 0.76. In demembranated fibers in rigor at low force (

UR - http://www.scopus.com/inward/record.url?scp=0041843694&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(03)74547-0

DO - 10.1016/S0006-3495(03)74547-0

M3 - Article

SN - 1542-0086

VL - 85

SP - 1098

EP - 1110

JO - Biophysical Journal

JF - Biophysical Journal

IS - 2

ER -