Protein folding

3.2 Folding analysis of recombinant TGF-β1 protein To analyze the folding of recombinant TGF-β1, purified protein was electrophoresed on native gel, under non-reducing condition and stained with the silver stain. Electrophoresis of the purified TGF-β1, under non-reducing condition, confirmed the presence of dimeric form of the TGF-β1, as a 25 kDa band on the non-denaturing gel (Figure 5 ). Here, there was no trace of a monomeric TGF-β1 band (13.5 kDa). This result indicated that the mature form

Implications of Improper Protein Folding in Alzheimer ’s Disease Stephen Sewell Schreiner University Dr. McGinnis Biochemistry Fall 2012 Abstract This paper is a brief review of the understanding of Alzheimer’s as it is generally seen today in the medical field, by scientists, physicians, and other healthcare providers alike. It examines the main hypothesis for the pathogenesis of the disease and the physical changes that the disease causes to the brain. The paper will then detail

Protein misfolding diseases include highly debilitating degenerative disorders like Alzheimer’s and Parkinson’s diseases. The healthcare and financial burden linked to these pathologies has been steadily increasing over the past decade. Actually, there is currently no efficient treatment for misfolding diseases as well as no reliable early diagnostic techniques for them, in most cases. It is known that, in many cases, the cytotoxic effect of misfolded proteins is exerted through their self-assembly

1.A. Original model of an essential amino acid Phenylalanine. This shows the atoms and bonds in both the backbone and the side chain. B. Original diagram of the different levels of protein structure (i.e., primary, secondary, tertiary, and quaternary). C. An original diagram, that demonstrates how a peptide bond is made through dehydration, using a complete chemical equation. Citation: Hudon-MIller

Proteins are complex macromolecules which are essential for life of all organisms. They are manufactured through the processes of transcription and translation, which take place inside the cells. More specifically, they are synthesised by ribosomes (Shakhnovich, 2007). Figure 1.1 shows the overall processes that can occur in making a fully functionally active protein. (Ghelis, 2012). Functional properties of certain proteins include, but is not limited to: structural composition of the cytoskeleton

saturate the outer region of a water soluble protein. They hydroxyl side chain can undergo glycosylation by adding saccharides and phosphorylation by adding phosphate through the actions of threonine kinase (New World Encyclopedia, 2015). B. Protein Structure C. Peptide bond through dehydration D. Peptide bond broken through hydrolysis E. Four forces that stabilize tertiary protein structure The tertiary structure is the last shape formation that a protein undergoes and is

functions of any compound. In biochemistry, structure dictates function. With the use of crystal structure analysis, scientists have a better way of analyzing specific proteins or enzymes and their function in our body. Observation of the human mitochondrial chaperonin is important because it assists in folding of mitochondrial proteins that allow for the production of energy in the cell. It also participates in specific process like apoptosis, inflammation and carcinogenesis. The study presents the

Lactate dehydrogenase is an enzyme that is found in most living organisms which catalyzes the conversion of lactate to pyruvic acid. It converts NAD+ to NADH and back again. Pyruvate is converted to lactate when oxygen isn’t present and the reverse reaction takes place (Wikipedia). There are two major subunits of lactate dehydrogenase which are the M form and the H form. The M form, major subunit in muscles, is efficient in the conversion of pyruvate to lactate. The H form, major subunit in the heart

Proteostasis is the way that organisms maintain protein fidelity in the body(Labbadia et al., 2015). It consists of multiple different mechanisms which help to coordinate protein synthesis, folding, disaggregation, and degradation(Labbadia et al., 2015). The multiple mechanisms that help to achieve proteostasis make up a system called the proteostasis network. This network incorporates all of the processes of proteostasis, including all machinery including translation, molecular chaperones, co-chaperones

biology conveys the idea that genetic information passes from DNA to RNA before ‘culminating in protein synthesis’ (Bandyra & Luisi, 2015). In essence, our genetic information is mainly used to code for specific proteins. There are 20 amino acids that can be bonded together in many different orders to form a number in excess of 10 million proteins across all biological organisms (Innovateus, 2015). Proteins have many different uses and functions, as well as modifications. Examples of these differences