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Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] The two most common secondary structural elements are alpha helices and beta sheets , though beta turns and omega loops occur as well.
Second normal form (2NF), in database normalization, is a normal form. A relation is in the second normal form if it fulfills the following two requirements: A relation is in the second normal form if it fulfills the following two requirements:
Codd introduced the concept of normalization and what is now known as the first normal form (1NF) in 1970. [4] Codd went on to define the second normal form (2NF) and third normal form (3NF) in 1971, [5] and Codd and Raymond F. Boyce defined the Boyce–Codd normal form (BCNF) in 1974. [6]
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.
1NF is a property of the individual values that appear in a database, the value domains; it doesn't say anything about the structure of a database or the relationships between values within a database. There is no standard way to mathematically formalize 1NF: if you want to do it, you have to do it in terms of constraints on values in domains ...
A hairpin is a special case of a turn, in which the direction of the protein backbone reverses and the flanking secondary structure elements interact. For example, a beta hairpin connects two hydrogen-bonded , antiparallel β-strands (a rather confusing name, since a β-hairpin may contain many types of turns – α, β, γ, etc.).
N mers form the polymer, whose total unfolded length is: =, where N is the number of mers.. In this very simple approach where no interactions between mers are considered, the energy of the polymer is taken to be independent of its shape, which means that at thermodynamic equilibrium, all of its shape configurations are equally likely to occur as the polymer fluctuates in time, according to ...
The chain has two ends – an amine group, the N-terminus, and an unbound carboxyl group, the C-terminus. [2] When a protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The amino end of an amino acid (on a charged tRNA) during the elongation stage of translation, attaches to the carboxyl end of the growing chain.