Title: Protein structure
Content:  There are four distinct levels of protein structure.
Title: Structure
Content:  In biology, one of the properties of life is its highly ordered structure, which can be observed at multiple levels such as in cells, tissues, organs, and organisms. In another context, structure can also observed in macromolecules, particularly proteins and nucleic acids. The function of these molecules is determined by their shape as well as their composition, and their structure has multiple levels. Protein structure has a four-level hierarchy. The primary structure is the sequence of amino acids that make it up. It has a peptide backbone made up of a repeated sequence of a nitrogen and two carbon atoms. The secondary structure consists of repeated patterns determined by hydrogen bonding. The two basic types are the α-helix and the β-pleated sheet. The tertiary structure is a back and forth bending of the polypeptide chain, and the quaternary structure is the way that tertiary units come together and interact. Structural biology is concerned with biomolecular structure of macromolecules.
Title: Biomolecular engineering
Content:  Proteins are polymers that are made up of amino acid chains linked with peptide bonds. They have four distinct levels of structure: primary, secondary, tertiary, and quaternary. Primary structure refers to the amino acid backbone sequence. Secondary structure focuses on minor conformations that develop as a result of the hydrogen bonding between the amino acid chain. If most of the protein contains intermolecular hydrogen bonds it is said to be fibrillar, and the majority of its secondary structure will be beta sheets. However, if the majority of the orientation contains intramolecular hydrogen bonds, then the protein is referred to as globular and mostly consists of alpha helices. There are also conformations that consist of a mix of alpha helices and beta sheets as well as a beta helixes with an alpha sheets. The tertiary structure of proteins 
Title: Protein quaternary structure
Content:  Protein quaternary structure is the fourth (and highest) classification level of protein structure. Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits). Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits. In contrast to the first three levels of protein structure, not all proteins will have a quaternary structure since some proteins function as single units. Protein quaternary structure can also refer to biomolecular complexes of proteins with nucleic acids and other cofactors.
Title: Biomolecular structure
Content:  Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels: primary, secondary, tertiary, and quaternary. The scaffold for this multiscale organization of the molecule arises at the secondary level, where the fundamental structural elements are the molecule's various hydrogen bonds. This leads to several recognizable domains of protein structure and nucleic acid structure, including such secondary-structure features as alpha helixes and beta sheets for proteins, and hairpin loops, bulges, and internal loops for nucleic acids. The terms primary, secondary, tertiary, and quaternary structure were introduced by Kaj Ulrik Linderstrøm-Lang in his 1951 Lane Medical Lectures at Stanford University.
Title: Jane S. Richardson
Content:  an article titled "The anatomy and taxonomy of protein structure" 1981, an early hallmark publication in structural bioinformatics. The diagrams have since become a standard way of visualizing protein structure, specifically depicting beta-sheet topology and connections between amino acid sequences, or peptides, that make up proteins. The protein folding process involves four levels: primary structures, secondary structures, tertiary structures, and quaternary structures. Secondary structures result from hydrogen bond interactions between adjacent amino acids sequences to form alpha helices or beta-sheets. Tertiary structures are a higher order of protein folding that depict the conformation of and connectivity between alpha-helices and beta-sheets in 3D. Richardson's ribbon diagrams illustrate beta-sheet topology and connectivity in 
Title: Structural bioinformatics
Content:  The structure of a protein is directly related to its function. The presence of certain chemical groups in specific locations allows proteins to act as enzymes, catalyzing several chemical reactions. In general, protein structures are classified into four levels: primary (sequences), secondary (local conformation of the polypeptide chain), tertiary (three-dimensional structure of the protein fold), and quaternary (association of multiple polypeptide structures). Structural bioinformatics mainly addresses interactions among structures taking into consideration their space coordinates. Thus, the primary structure is better analyzed in traditional branches of bioinformatics. However, the sequence implies restrictions that allow the formation of conserved local conformations of the polypeptide chain, such as alpha-helix, beta-sheets, and loops (secondary structure ). Also, weak interactions (such as hydrogen bonds) stabilize the protein fold. Interactions could be intrachain, i.e., when occurring between parts of the same protein monomer (tertiary structure), or interchain, i.e., when occurring between different structures (quaternary structure).
Title: Protein quinary structure
Content:  Protein quinary structure refers to the features of protein surfaces that are shaped by evolutionary adaptation to the physiological context of living cells. Quinary structure is thus the fifth level of protein complexity, additional to protein primary, secondary, tertiary and quaternary structures. As opposed to the first four levels of protein structure, which are relevant to isolated proteins in dilute conditions, quinary structure emerges from the crowdedness of the cellular context, in which transient encounters among macromolecules are constantly occurring. In order to perform their functions, proteins often need to find a specific counterpart to which they will bind in a relatively long encounter. In a very crowded cytosol, in which 
Title: Protein structure
Content:  Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds. Despite the fact that there are about 100,000 different proteins expressed in eukaryotic systems, there are many fewer different domains, structural motifs and folds.
Title: Protein
Content:  the aid of molecular chaperones to fold into their native states. Biochemists often refer to four distinct aspects of a protein's structure: Proteins are not entirely rigid molecules. In addition to these levels of structure, proteins may shift between several related structures while they perform their functions. In the context of these functional rearrangements, these tertiary or quaternary structures are usually referred to as "conformations", and transitions between them are called conformational changes. Such changes are often induced by the binding of a substrate molecule to an enzyme's active site, or the physical region of the protein that participates in chemical catalysis. In solution proteins also undergo variation 

Question: how many levels of protein structure are there?
Answer: four.