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
Amino acids are the building blocks of proteins. All amino acids have the same basic structure but differ in their R-side chains. Each amino acid consists of an amino group (-NH3), a carboxyl group (-COOH) and a hydrogen atom (H). The amino and carboxyl groups are attached to a central alpha carbon together with a hydrogen atom and an R-side chain. There are currently known that over 170 amino acids occur in organisms but only 20 are commonly found in proteins.
Proteins are amphoteric in nature. Protein Structure Protein has four different structures: Primary Secondary Tertiary Quaternary Functions of Proteins in the human body : Proteins are used for repair and maintenance of body tissues. Also for growth of hair and nails. Proteins provide a major source of energy Proteins are involved in the manufacture of some hormones. Proteins are a major element in the transportation of certain molecules.
This chapter presents an overview of protein structure prediction by representing some of the techniques. The structure prediction of protein has two main techniques. The secondary structure prediction and tertiary structure prediction methods are also discussed in this chapter. 2.1 OVERVIEW OF PROTEIN STRUCTURE PREDICTION TECHNIQUES Proteins perform many biological functions and represent the building blocks of organisms. Basically there are 20 types of amino acids in proteins consists of different chemical properties.
This is between the deoxyribose sugar of one nucleotide and the phosphate component of the other nucleotide, which brings about the alternating sugar phosphate backbone.All biological information is stored in DNA which makes every organism unique. There are pieces of DNA called genes which determine a particular trait in a living organism.The sugar phosphate backbone of the DNA resist against cleavage, and both double helical strands stores the biological information, which is transcribes / replicated as they separate. These DNA strands are anti-parallel to each other as they run from and are transcribed from a 3-5 end. They are similar but they run in opposite directions. The 5(prime) carbon would be located at the top of the leading strand which is replicated continuously and the carbon on the other end, where on the lagging strand the 3(prime) carbon is at the lower portion where these are replicated in sections known as Okazaki fragments.
Tannins have a very high affinity for proteins and form protein-tannin complexes. The ingestion of a plant containing condensed tannins decreases nutrient utilization, protein being affected to a great extent, and decreases feed intake. On the other hand, hydrolysable tannins are potentially toxic to animals. Consumption of feeds containing high levels
1. Introduction: a. Hemoglobin structure: Hemoglobin is metalloprotein found in red blood cells having four polypeptide chains. Adult hemoglobin contains 2 alpha (141amino acid) and 2 beta chains (146 amino acid) which forms a tetramer called as globin and each chain is attached to iron containing prosthetic group heme (protoporphyrine IX). Ferrous ion of this heme is linked to globular protein by binding ‘N’ in the center of the protoporphyrin ring. There is a non-covalent interaction between four chains.
ABSTRACT Gamma secretase enzyme is a multi-subunit proteinase complex, an integral membrane protein that severs single-pass transmembrane proteins at residues intervals the transmembrane domain. The most substrates of γ- secretase are amyloid precursor protein (APP), an outsized integral membrane macromolecule that, once cleaved by each γ-and β-secretase, produces 39-42 amino acid amide known as amyloid beta whose abnormally folded fibrillar type is that the primary part of amyloid plaques found in the brains of Alzheimer's disease (AD) patients. The gamma-secretase complex consists of 4 individual proteins: presenilin, PEN-2 (presenilin enhancer 2), APH-1 (anterior pharynx-defective 1), nicastrin. We know the structure of 2 subunits presenilin and
Steered molecular dynamics (SMD) simulation has been used to apply external force on certain atoms in specific pulling direction in silico, which is perfect for pulling the knotted proteins. Sułkowska et al have stretched 20 proteins with a knotted topology by SMD simulations using a coarse-grained model. (105) When a stretching force is applied onto the two ends of a knotted protein, the knot shrinks and one end of the knot move along the polypeptide chain with sudden jumps. This is quite different from the tightening of a homopolymer in which the knot
On the outer arms the dyneins are the same with three different heavy chains. The dynein also has a flexible stem, globular head as well as a thin string with the ATP binding site. Axonemal dynein proteins cause microtubules to move and thus the cilia and flagella move by a beating process. Cilia and flagella have very similar structure so it is very difficult to distinguish them from each other at times. However we can distinguish between them from their movement.
1. How does DNA encode information? DNA is a double-stranded helix composed of a phosphate backbone and deoxyribose, and encodes information by the sequence of its nucleotide bases, which are composed of adenine, thiamine, guanine and cytosine. DNA undergoes transcription, which produces single-stranded mRNA, which uses uracil in place of thiamine. Next step is translation, in which the RNA becomes a protein, which then can act as structural units or enzymes.
Macromolecules are usually used to refer to large biological polymer which are made up of small monomers linked together. All living things contain organic macromolecules, which is divided into four main groups: Lipids, proteins, carbohydrates and nucleic acids. (D 'Onofrio, 2009-2015) Characteristic for these organic molecules is that they are made up of only a small number of elements: carbon, hydrogen, oxygen, and to smaller amounts nitrogen, phosphorus and sulfur. Carbohydrates are better known as sugars and starches. There are three main categories in which carbohydrates can be divided into: Monosaccharides, disaccharides and polysaccharides.