# THICK FILAMENT MYOSIN AND C-PROTEIN ARRANGEMENT

> **NIH NIH R01** · UNIVERSITY OF MISSOURI KANSAS CITY · 1990 · $123,642

## Abstract

The arrangement of myosin and accessory protein such as C-
protein in the thick filaments of fish, avian, and mammalian
skeletal muscles is still not clearly elucidated.  Recent work in
our laboratory on the structure of frog thick filaments however,
has demonstrated that the structure of vertebrate muscles may be
amenable to analysis by a combination of electron microscopy,
optical diffraction analysis, and computer image analysis.
Additionally, it has been shown that thick filaments from fich,
avian, and mammalian muscle can be isolated with a similarly
well ordered array of crossbridges; thus making these filaments
suitable for analysis by the same type of techniques which have
proven useful for the frog thick filaments.  The specific aim of
the proposed research is to extend the techniques used for the
frog thick filaments to the determination of the structure of the
thick filaments of fish, avian, and mammalian skeletal muscles.
The major objective of theses studies will be the determination of
the arrangement of the myosin and accessory proteins in the
filaments of these vertebrate classes.  The studies to accomplish
these aims will include: 1) the use of a combination of negative
staining, platinum shadowing, rapid-freeze deep-etch cryo studies,
and optical diffraction analysis to elucidate the major
ultrastructural features of the filaments and to assess the
preservation of the filaments as compared to the structural
parameters expected from X-ray diffraction patterns of living
muscle; 2) the use of computer image analysis of the filament
images in the best electron micrographs to determine the
rotational symmetry and arrangement of the myosin heads, and to
produce a three-dimensional reconstruction of the structure of
the filament; 3) the use of immunolabelling studies to determine
the probable location of accessory proteins such as C-protein and
X-protein on the filaments, and to correlate this information with
the structure of the filament as seen in the three dimensional
reconstructions.  These studies will provide basic scientific
information about the structure of muscle, and will thus provide a
better foundation for understanding how pathological conditions
may affect the functioning of this tissue.

## Key facts

- **NIH application ID:** 3155808
- **Project number:** 5R01AR030442-10
- **Recipient organization:** UNIVERSITY OF MISSOURI KANSAS CITY
- **SAM.gov UEI:** J9CDGR596MN3
- **Principal Investigator:** Robert W. Kensler
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $123,642
- **Award type:** 5
- **Project period:** 1988-10-01 → 1992-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3155808

## Citation

> US National Institutes of Health, RePORTER application 3155808, THICK FILAMENT MYOSIN AND C-PROTEIN ARRANGEMENT (5R01AR030442-10). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3155808. Licensed CC0.

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