Abstract
In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)), being biologically active, do not have a specific 3D-structure in their unbound states under physiological conditions. There are also subtler categories of disorder, such as conditional (or dormant) disorder and partial disorder. Both the ability of a protein/region to fold into a well-ordered functional unit or to stay intrinsically disordered but functional are encoded in the amino acid sequence. Structurally, IDPs/IDPRs are characterized by high spatiotemporal heterogeneity and exist as dynamic structural ensembles. It is important to remember, however, that although structure and disorder are often treated as binary states, they actually sit on a structural continuum.
Highlights
Other small disordered segments called Molecular Recognition Features (MoRFs) [26], which undergo a contextual transition between disorder and order upon binding, have a function that is defined by the presence of disorder and the transition to an ordered state, and not by a defined three-dimensional structure
True negatives (TN) and false positives (FP)/false negatives (FN) is the objective, and this is typically expressed by the Matthews Correlation Coefficient (MCC)
This allows the enzyme to translocate the catalytic domain across the narrow type 1 secretion involved in disease pathogenic protective capacities willgradient emergeonwith channel, and thenprocesses transition in to aboth globular structureand when exposed to the calcium the the increased acceptance of the functional roles that intrinsically disordered protein regions (IDPRs) in enzymes may play
Summary
The dominant paradigms in protein science were, in many ways, shaped by the earliest experiments in the field. Protein behavior, where well-behaved well-behaved was synonymous with well-structured, with one singular function, and one mechanism of action In many ways, these these early early experiments experiments represented canonical examples of how proteins should be, which all further experiments were held against. Results that ran counter to this assumption were typically considered a problem with the experiment experimenter, and not aa result result of of the the intrinsic intrinsic properties properties of of the the protein As these these anomalies anomalies or the experimenter, accumulated to the point where they could no longer be ignored, these problem proteins and problem regions were often seen as functionally irrelevant, and and in in many many cases, cases, removed removed before before experimentation
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