A macromolecule is the large molecules necessary for life, include carbohydrates, lipids, nucleic acids, and proteins. Protein has four levels to its structure; Primary, Secondary, Tertiary, and Quaternary. Primary is a straight chain, Secondary is held by hydrogen bonds, Tertiary is called subunits, and Quaternary is composed of two or more subunits. Two examples of proteins are actin and collagen. “Actin is a globular multi-functional protein that forms microfilaments. It is found in essentially all eukaryotic cells.”(NCBI. NMH) “Collagen is a part of the connective tissue that in the skin helps in firmness, suppleness and constant renewal of skin cells.”(News Medical Net). The process of monomers joining to form polymers is called dehydration
Proteins are complex macromolecules that are formed by elements carbon, hydrogen, oxygen and nitrogen. Proteins composed of one or more polypeptide chains of amino acids. The main functions of proteins are to structure, support, protect, make movement, catalyst, transport and make hormones in human body. In the structural role, collagen and elastin provide support for connective tissue. Actin and myosin are proteins that involved in muscle contraction and movement.
Proteins are a chain of amino acids, and are found in all living things. Using the methods of x-ray crystallography, he solved the basic structure of proteins. His work with protein lead to the discovery of the Alpha helix, which is formed by hydrogen bonding and twists the protein shape into a spiral. The founding of molecular biology and protein structure sparked an interest in hemoglobin, and in no time Pauling was making discoveries with regards to hemoglobin. Hemoglobin is a protein found in red blood cells and is essential for the transport of oxygen throughout the human body ().
The cytoskeleton also allows organelles to move around within the cell by providing tracks with its protein filaments. This is important as it ensures the correct concentration of the required components is kept at the different sites within the cells. The 3 classes of filaments that make up the cytoskeleton are polymers made up of protein sub-units. The microtubules are the largest and provide the cell with its dynamic shape. It is these fibres that undergo continual assembly and disassembly.
Amino acid play central roles as building blocks of proteins and as intermediates in metabolisms . The 20 amino acids are found within proteins convey a vast array of chemical versatility (The Biology Project.2000).All amino acids found in proteins have a basic structure , different only in the structure of the R group or the side chain(Figure). In this basic structure amino acid (Figure 4 ) is containing a central C atom , in sides a H atom, an amino group, a carboxyl group and the R group. The amino acid can be recognized based on this R group .
SOPHIA COLLEGE Protein-DNA Interaction MAYUR GAIKWAD 05/05/2015 INTRODUCTION Protein–DNA interactions play a major role in all fields of genetics from regulation and transcription of individual genes to repair of damaged sequences, even to the stabilization of DNA in chromatin and the replication of entire genomes. It is estimated that 2–3% of prokaryotic and 6–7% of eukaryotic genes code for DNA-binding proteins. Additionally, many of these proteins do not merely bind DNA, but also interact with other proteins and sometimes, as is shown in the example of RNA polymerase, only display theirfull activity when organized in multimeric complexes.
Its role is to act as a medium in the cell. The cytoplasm has a large amount of organelles also known as little organs. Large protein molecules called enzymes are found in both the cytoplasm and in the organelles. Enzymes carry out many chemical reactions in order to create energy, they also transform raw materials into useful substances, or break down old proteins to be recycled.
After this optimum is exceeded, the reaction rate sharply decreases to 1 mL/minute during pH 10 and 12. This reduction of activity can be explained through the act of denaturing. This occurs when the enzyme’s tertiary structure collapses, as the hydrogen bonds that form the protein begin to break apart. The function of proteins is heavily reliant on its structure, and once it deforms, it becomes ineffective. In this particular scenario, the active of the enzyme will alter and its once complementary substrate is unable to bind, preventing the reaction from
This theory evolved from studies of peptides synthesized according to sequences of SP-B amino acids or mimicking these sequences which showed that SP-B provided cohesiveness to molecules of phospholipids (Cochrane, 2005; Cochrane and Revak, 1991). The peptides and SP-B are hydrophobic and are positioned in the acyl side chains of the phospholipid monolayer, with strong electrostatic interactions between the positively charged amino acids and the negatively charged phospholipids. This bonding of SP-B, peptide and phospholipid molecules confers lateral stability to the phospholipid molecules in the monolayer of the alveolus and by virtue of this; the cohesive monolayer is able to prevent collapse of the alveolus (Cochrane, 2005; Mazela et al.,
What is a mitochondrion and what significance does it hold for the basis of molecular biology? To put it simply, a mitochondrion is and organelle commonly found in large numbers in the majority of cells. The Mitochondrion is responsible for biochemical processes such as, respiration, oxidative phosphorylation and ATP synthesis. Thus, the Mitochondrion, or mitochondria accountable, are known as ‘ATP factories’ or ‘the powerhouse’ of the cell. It is obvious as to why mitochondria were studied in such detail.
The residue in favoured region and also the allowed regions are found to be 91.40 % and 6.0 % of the total residues respectively. This show good interaction of subunit structures to form the complex structure of γ-secretase. Docked result of all the subunits (1044residues) Number of Residue Percentage of the total Favoured Region 954 91.4 Allowed Region 63 6.0 Outlier Region 27 2.6 Table.6: Ramachadran plot analysis of the tertiary structure generated using all the subunits of the gamma-secretase Figure.13: Ramachandran plot of the tertiary structure generated from all the subunits of gamma-secretase. DISCUSSION AND FUTURE PERSPECTIVE Swiss PDB Viewer