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To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology , which employs techniques such as X-ray crystallography , NMR spectroscopy , cryo-electron microscopy (cryo-EM) and dual polarisation interferometry ...
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 ...
Protein quaternary structure [a] 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).
A specific nonlinear optical technique called second-harmonic generation (SHG) has been recently applied to the study of conformational change in proteins. [4] In this method, a second-harmonic-active probe is placed at a site that undergoes motion in the protein by mutagenesis or non-site-specific attachment, and the protein is adsorbed or ...
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.
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.
This movie depicts the 3-D structures of each of the representative conformations of the Markov State Model of Pin1 WW domain. In computational chemistry, conformational ensembles, also known as structural ensembles, are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.
Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...