Protein fold classIn molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). Four large classes of protein that are generally agreed upon by the two main structure classification databases (SCOP and CATH).
Intrinsically disordered proteinsIn molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain proteins. They are sometimes considered as a separate class of proteins along with globular, fibrous and membrane proteins.
Entropic forceIn physics, an entropic force acting in a system is an emergent phenomenon resulting from the entire system's statistical tendency to increase its entropy, rather than from a particular underlying force on the atomic scale. In the canonical ensemble, the entropic force associated to a macrostate partition is given by where is the temperature, is the entropy associated to the macrostate , and is the present macrostate.
Maximum length sequenceA maximum length sequence (MLS) is a type of pseudorandom binary sequence. They are bit sequences generated using maximal linear-feedback shift registers and are so called because they are periodic and reproduce every binary sequence (except the zero vector) that can be represented by the shift registers (i.e., for length-m registers they produce a sequence of length 2m − 1). An MLS is also sometimes called an n-sequence or an m-sequence. MLSs are spectrally flat, with the exception of a near-zero DC term.
