This document discusses the structure, functions, and properties of proteins. It describes the primary, secondary, tertiary, and quarternary levels of protein structure. Misfolded proteins can lead to diseases like Alzheimer's and Parkinson's.
This document discusses the structure, functions, and properties of proteins. It describes the primary, secondary, tertiary, and quarternary levels of protein structure. Misfolded proteins can lead to diseases like Alzheimer's and Parkinson's.
This document discusses the structure, functions, and properties of proteins. It describes the primary, secondary, tertiary, and quarternary levels of protein structure. Misfolded proteins can lead to diseases like Alzheimer's and Parkinson's.
This document discusses the structure, functions, and properties of proteins. It describes the primary, secondary, tertiary, and quarternary levels of protein structure. Misfolded proteins can lead to diseases like Alzheimer's and Parkinson's.
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Protein Chemistry is a diverse field of studying and understanding the
function, structure, chemical properties, uses, and interactions of proteins. Proteins are complex molecules that play an essential role to make human cells, tissues, and organs function well. They are made of chains of smaller units of amino acids to form a poly-peptide chain that can help in various biological processes such as enzymatic reactions, cellular signaling, and structural support. According to MedlinePlus (2021), proteins are responsible for most of the work in the human body such as structure, function, and regulation. There are 20 different types of amino acids combined to produce proteins. Its sequence represents the protein’s 3D structure and functions.
The National Library of Medicine
(2004) stated that the complete structure of a protein is divided into four levels: primary, secondary, tertiary, and quarternary. Khan Academy (2022) simply defines primary structure as the sequence of amino acids. One example of a protein that has a primary structure is the insulin. It is composed of two polypeptide chains, A and B. Chain A and B has their sequence of amino acid. Anfinsen (1973) demonstrated that the way the protein folds and interacts with itself and other molecules is determined by the primary structure. However, some factors like temperature changes, pH, and the presence of other molecules can interrupt the process of folding and its shape which affects the protein’s function.
According to Sneha et.al.
(2016) in their study Advances in Protein Chemistry and Structural Biology, secondary structure of a protein refers to the ways of different regions of poly-peptide chains to fold and interact with other molecules through hydrogen bonds. It also plays a big role in predicting the tertiary structure of proteins. There are two common forms of secondary structure: alpha-helix and beta-helix. Alpha-helices are held together by hydrogen bonds in the poly-peptide backbone which causes the helix to coil in the right direction. Beta-pleated sheets on the other hand are held together by hydrogen bonds in different poly-peptide backbone. The chains of beta-pleated sheets are aligned parallel or anti-parallel to each other (Boundless, 2020).
BD Editors (2020) described the tertiary structure of
protein as the 3-Dimensional shape resulting from the process occurred in the secondary structure. This structure is important in determining the function of the protein. In this structure, the folding of the polypeptide chain will be a complex process so it should be assisted by chaperones. Chaperonse are specialized proteins that helps in preventing incorrect folding. They are responsible in moving or manipulating the protein around, bringing different types of amino acids closer together which then can form bonds to form the 3- Dimensional structure.
The quarternary structure according to
Byju (2023) is the result of the process done in tertiary structure. The quarternary structure is produced by the arrangement of these subunits with respect to each other.
In the process of folding, there
are some errors that may occur. Misfolded proteins can lead to some diseases such as Huntington’s, Parkinson’s, and Alzheimer’s. Raynaud (2010) stated that the function of proteins depends on their native conformation or folding it into the 3- Dimensionl structure. If misfolding occurs spontaneously, it can lead to the formation of toxic protein folds, that results in several diseases. This misfolded protein follows the wrong folding pathway leading to the formation of an incorrect conformation.
As there are many differentiating properties of proteins, determining their
characteristics and structure is important. To further develop an understanding of what proteins are, this qualitative research aims to discuss the functions, structure, and characteristics of proteins.
REFERENCES
Anfinsen (1973). Principles that govern the folding of protein chains. Science, 181(96), 223-230. https://doi.org/10.1126/science.181.4096.223
BD Editor. (2020). Tertiary Structure - Definition and Function. Biology Dictionary. Retrieved from https://biologydictionary.net/tertiary-structure/
Boundless. (2020). Proteins - Protein Structure. In General Biology. LibreTexts.
Khan Academy (2022). Orders of protein structure. Khan Academy. Retrieved April 27, 2023, from https://www.khanacademy.org/science/biology/macromolecules/proteins-and- amino-acids/a/orders-of-protein-structure MedlinePlus (2021). How Genes Work: Protein Production. MedlinePlus. Retrieved April 27, 2023, from https://medlineplus.gov/genetics/understanding/howgeneswork/protein/
National Library of Medicine (2004). Overview of Protein Structural and Functional Folds. Retrieved April 27, 2003 from https://www.ncbi.nlm.nih.gov/pmc/articles
Reynaud, E. (2010). Protein Misfolding and Degenerative Diseases. Nature Education 3(9):28
Sneha, P. et.al. (2016). Protein secondary structure. In Advances in Protein Chemistry and Structural Biology (Vol. 105, pp. 19-48). Elsevier. Retrieved April 27, 2023 from https://www.sciencedirect.coma
2019 - Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding
