# MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISM

> **NIH NIH R01** · BRANDEIS UNIVERSITY · 1987 · $282,226

## Abstract

The objective of this program is to determine the precise molecular
architecture of a diverse class of Alpha-fibrous proteins whose role is
both structural and dynamic.  The chief methods are coordinated X-ray
crystallography, electron microscopy and image analysis.  Muscle proteins
are a central focus and provide the background for studying related
systems.  A major aim is to determine the structure and motions in two
calcium-dependent protein switches that control contraction.  Thus crystals
of the regulatory complex tropomyosin/troponin are being analyzed, and the
topology of the myosin molecule with its associated light chains will be
determined to establish models for regulation.  The molecular basis of
blood clotting is being studied by a similar approach.  The structure of
fibrinogen will be determined by X-ray crystallography and its packing
established in the fibrin clot.  These structural methods will also be
applied to certain cytoskeletal and cell surface proteins (including those
on human parasites) that play important roles in cell form, movement and
interactions.  The broad study of these systems is directed towards
identifying distinctive features of structure that are essential to their
function.

Knowledge of the molecular mechanisms of contraction and its regulation in
normal muscle is needed to account for their failure in various heart and
muscle diseases.  Similarly, a full understanding of blood clotting, and
its malfunction in certain cardiovascular diseases, requires detailed
information about the structure and interactions of the fibrinogen
molecule.  We now recognize the vital role of the cytoskelton and various
arrays of internal and external cell surface proteins in normal cell
function and in development, and the responsiveness of these structures to
cell transformation.  The occurrence of fibrous proteins that may be
related to muscle proteins at the surface of pathogenic organisms has
important medical implications.  We believe that our broad study of the
structure and interactions of these fibrous proteins will lead to a deeper
understanding of both normal and abnormal cellular function.

## Key facts

- **NIH application ID:** 3154953
- **Project number:** 5R01AR017346-15
- **Recipient organization:** BRANDEIS UNIVERSITY
- **SAM.gov UEI:** MXLZGAMFEKN5
- **Principal Investigator:** CAROLYN COHEN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $282,226
- **Award type:** 5
- **Project period:** 1974-09-01 → 1989-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154953

## Citation

> US National Institutes of Health, RePORTER application 3154953, MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISM (5R01AR017346-15). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3154953. Licensed CC0.

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