Basically there are 20 types of amino acids in proteins consists of different chemical properties. A long chain of these amino acids forms the protein molecule with the neighbor through a covalent peptide bond. Proteins are also known as polypeptides. Protein folding is the collection of proteins into larger structures
INTRODUCTION Protein folding is a process by which a polypeptide chain folds into its native three dimensional structure, a conformation that is biologically functional. It is most often assumed that protein folding and its biophysical and structural properties observed in dilute buffer solutions in vitro also represent the in vivo scenario. However the intracellular environment is highly crowded because of the presence of large amounts of soluble and insoluble biomolecules including proteins, nucleic acids, osmolytes, ribosomes and carbohydrates. [reference] It has been estimated that the concentration of macromolecules in the cytoplasm ranges from 80 to 400 mg/ml [life in crowded world, rivas, 2004]. All macromolecules in physiological fluids
The electron density for X is mostly consistent with N, C, or O, but efforts to identify this atom have yet to be successful. FeMo-cofactor is anchored to the MoFe protein by α-275Cys to an iron atom at one end and α-442His to the Mo atom at the other end (Figure
DNA is a negatively charged macro molecule. Protein interact with the DNA with its positively charged residues. Protein molecule interact with DNA by means of hydrogen bonding mainly. The hydrogen bonding play an essential role for many bio-molecular interaction. We can found this kind of interaction during protein-protein interaction, DNA protein interaction, enzyme
Protein-protein interaction refers to the physical contact between two or more proteins that result in a biological function. These interaction often take the form of molecular machines that carry out a diverse number of essential physiochemical processes. Specific interactions between the proteins of host and pathogen forms the primary basis of infection. The proteins involved in such interactions are referred to as ‘host-pathogen interactomes’. 1.2.2 Significance of PPI: Surface proteins of both the host and pathogen that are involved in such interaction play a key role in the initiation of infection.
Secondary structure: areas of folding or coiling within a protein with examples include alpha helices and pleated sheets, which are stabilized by hydrogen bonding. Tertiary structure: the final three-dimensional structure of a protein, which results from a large number of non-covalent interactions between amino acids. Quaternary structure: non-covalent interactions that bind multiple polypeptides into a single, larger protein. Hemoglobin has quaternary structure due to association of two alpha globin and two beta globin polyproteins. 2.3
Polar amino acids ( acidic, basic, neutral) are hydrophilic & tend to be placed on the out side of the protein. Non-polar ( Hydrophobic) amino acid tend to be placed on the inside of the proteins. It is the fundermental level of protein structure. Its explain the unit amino acid sequence of form carboxyl terminals to amino acid terminal in a protein. Primary structure is very important as it indicates the 3 dimentional structure needed for the biological function of protein.
Deoxyribose nucleic acid (DNA) is present in the nucleus of all living organisms. It controls all the chemical changes within the cell and determines the kind of organism that is produced. Each cell is identical (unless specialised) and contains the genetic information of the living organism. DNA consists of a double strand of nucleotides, the sugar-phosphate chains are parallel to each other, and these chains are held together by bonds between the bases. Nucleotides are made up of three parts; a sugar base called ribose, a phosphate groups and an organic/nitrogenous base.
These isoprene chains also contain branching methyl side chains, which can interact with the plasma membrane in surprising ways. The first difference is the chirality of glycerol. Bacteria and eukarya possess D-glycerol, while archaea have L-glycerol. These terms are in fact historical, their actual names being sn-glycerol-3-phosphate and sn-glycerol-1-phosphate; respectively. These names also encompass the