Protein structure

1.3 Identifying Knotted Proteins The complexity of protein folding makes it very challenging to fully understand the folding mechanism of proteins. More complex yet interesting challenges have been proposed. One of the most interesting challenges is the protein with knotted topology.(9-12) Knot is very common in our daily life. Sometimes we hate the knot and need to untie it. For example, our earphone cable often gets knotted and it takes forever to untie it. But, more often, we need the knot,…

BIOL 3612 Biochemistry Lab EXERCISE 1: SOME BASICS OF SECONDARY AND TERTIARY STRUCTURE Exploring PDB files and secondary structure The exercise was helpful in creating a picture for me to really understand the 3D structures of proteins. By navigating through different protein representations, I was able to recall several important concepts I learned from lecture. Also, by seeing those structures in relative to one another, I was able to putting the concepts together…

four types of interactions that stabilize a protein and give it structure at the tertiary level. Hydrophobic interactions are nonpolar molecules, they generally have a long chain of carbons that do not interact with water molecules. RGroups prefer to interact with each other internally and away from water (Wolfe, G. (2000). Thinkwell biochemistry - 2.7.4 Tertiary Structure). This interaction contributes significantly to the folding and shaping of a protein. Hydrophobic interactions are…

carbohydrates, lipids, proteins and nucleic acids. Carbohydrates contain carbon, hydrogen, and oxygen, as well as provide a means for energy and cell support in plants. .( Parsi et al, 2016) They can be further categorized by the subtitles monosaccharides, disaccharides, and polysaccharides. Since monosaccharides are monomers and thus simple sugars, as monomers are added to the chain they become polysaccharides. In addition starches and glycogens are polysaccharides. .( Parsi et al, 2016)…

FOXO proteins are the O class of the Forkhead family of proteins. Forkhead protein (FOX) was first discovered in Drosophila and when mutated results in a head structure that resembles a fork (Wiegel et al 1989). Over 100 FOX proteins have been identified since and classified as FOXA to FOXR depending on sequence similarities. The FOX family of proteins function as transcription factors and their defining feature is a DNA binding domain known as the fork head domain (Lai et al 1993). This domain…

expected that pepsin will destroy the structure of gelatin protein, because the pepsin broke down the primary structure of the gelatin polypeptide into amino acid monomers. The hydrochloric acid (HCL) expected to affect the ability of amylase to digest starch, because as it is an acid it effects on the protein that makes it unraveled as it breaks down the secondary structure which it contains hydrogen bonds. As I have done to experiment one titled Digestion of Proteins by Pepsin. The result was…

The full name of EHBP1 is "EH domain binding protein 1." The symbol for the gene is EHBP1. Other names for the EHBP1 gene are HPC12, NASCIN, and KIAA0903. EH Domain Binding Protein 1 is a protein coding gene. This gene codes for an Eps15 homology domain binding protein. Its protein type is a vesicle. The encoded protein may play a role in endocytic trafficking. It is associated with prostate cancer. This gene is commonly found within the cytosol and the plasma membrane of a cell. It's size is…

In protein synthesis there are 3 to 4 structures that occur. In the primary structure there are covalently bonded sequences of amino acids and this happens through dehydration synthesis where complex molecules are broken down to simple components. Secondary structure happens within the protein and can repeat multiple times and this happens from the folds by the Hydrogen bonds. Finally, you reach tertiary structure where the final 3-dimensional shape is shown by the complete polypeptide chain.…

A protein has a precisely defined amino acid sequence which gives rise to its three dimensional structure which is essential to the protein’s function. These amino acids interact with one another to produce a specific folding pattern that produces the conformation of the protein. When one looks at the progression a protein makes in its folding complexity, it is clear that the folding is driven by the amino acid sequence alone. To understand this concept it is best to start with the primary…

partners of CHIP: In section 3, after " fate of substrates": E2’s are the family of enzymes, having highly conserved ubiquitin conjugating domains. These enzymes, in combination with E3s, play an important role in determining the fate of substrate proteins by selecting a lysine residue on which ubiquitin moiety must be added. In section 3, after Murata, et al. 2003: An in vitro study has shown that CHIP, with the aid of UbcH5 and UbcH6, two other E2s, can efficiently ubiquitinate interferon…