Types of Proteins in the Muscle, Research Paper Example

Main Post: Types of Proteins in the muscle: microscopic structures- thin, thick, and other.

Research

The muscular tissue in the body is made up of different proteins, which have varietal functions (American Meat Science Association, 2015, para 1). Through electro-microscopy (EM), muscle tissues can easily be monitored and studied. Research through EM shows more structures, thin and thick filaments. The filaments are for muscle movements. The contraction happens between thin and thick structures(Craig, 2017, para 2). The thin structures are referred to as actin, whereas the thickones are collectively referred to as myosin. EM reveals that muscle contraction happens when thick slides over the thin filament without a length change. In addition, the two structures are parallel. Actin and myosin are proteins used in the contraction or shrinking and slackening of the muscles.

The protein in muscles can be grouped into three categories, myofibrillar, stromal, and sarcoplasmic. These categories have functional differences. Myofibrils make up muscle fibers, which are muscle cells organized into muscle bundles. The myofibrillar proteins are a group of proteins that make up the myofibril, including actin, myosin, and a few others. Actin and myosin are the most useful myofibrillar protein components for muscle fiber formation.

Moreover, myofibrils are made of series-linked sarcomeres (Biga et al., para 5). They are the most prevalent proteins in muscular tissue and directly participate in muscular contraction and relaxation. The region surrounding the myofibrils is the one that is known as sarcomeres. Stromal proteins are comprised of reticulin, collagen, and elastin, and these are connective tissues made of watery substances in which fibrils are dispersed. Sarcoplasmic proteins are made up of hemoglobin and myoglobin pigments, which play a role in the red coloring of the blood.

The electrostatic blockage model of thin filament regulation was established through newer imaging, X-Ray, and EM technologies. Research under these imaging techniques suggested that when the calcium ions were lower, tropomyosin, one of the thin muscle filaments, laid on actin in a location that physically prohibited myosin filaments from attaching to it. The azimuthal migration of tropomyosin was supposed to expose the myosin binding site at high calcium ions, facilitating the myosin, carrier protein binding, and muscle-contraction to occur (Craig, 2017, para 5).

In conjunction with tiny auxiliary protein, Myosin polymers make up thick filaments. The polymer has two hefty chains that are identical. Their C-terminal halves create a long, coiled-coil tail, while the filaments fold into a globular head in respective N-terminal halves. The C- and N- terminals are the myosin structures observed through the named imaging techniques(EM). The heads are flexibly attached to the tail and linked to two light chains. This molecular structure was initially discovered using electron microscopy (Craig, 2017, para 7).

Critical Thinking

Muscles are made of proteins. Eating meat, which is made up of muscular animal tendons or muscles, increases protein in a person’s body. That’s the reason for the protein being referred to as bodybuilding food. Actin and myosin are very important, as seen in the text, and they are useful during the contraction and relaxation of muscles. EM technology has been a game-changer in anatomy. The human body is complex; every tissue or organ or body part seems to be complex in itself.

References

American Meat Science Association. (2015). Does Muscle Tissue Contain Different Types of Protein? https://meatscience.org/TheMeatWeEat/topics/fresh-meat/article/2015/07/31/does-muscle-tissue-contain-different-types-of-protein

Biga L. et al. Anatomy & Physiology: 10.2 Skeletal Muscle. https://open.oregonstate.education/aandp/chapter/10-2-skeletal-muscle/

Craig R. (2017). Molecular structure of muscle filaments determined by electron microscopy. Applied microscopy, 47(4), 226–232. https://doi.org/10.9729/am.2017.47.4.226