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Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable three-dimensional structure, but rather adopt many different conformations in dynamic equilibrium. The interplay between local dynamics and global rearrangements is key for their function. In IDPs, proline residues are significantly enriched. Given their unique physicochemical and structural properties, a more detailed understanding of their potential role in stabilizing partially folded states in IDPs is highly desirable. Nuclear magnetic resonance (NMR) spectroscopy, and in particular C-detected NMR, is especially suitable to address these questions. We applied a C-detected strategy to study Osteopontin, a largely disordered IDP with a central compact region. By employing the exquisite sensitivity and spectral resolution of these novel techniques we gained unprecedented insight into cis-Pro populations, their local structural dynamics and their role in mediating long-range contacts. Our findings clearly call for a reassessment of the structural and functional role of proline residues in IDPs. The emerging picture shows that proline residues have ambivalent structural roles. They are not simply disorder promoters but rather can, depending on the primary sequence context, act as nucleation sites for structural compaction in IDPs. These unexpected features provide a versatile mechanistic toolbox to enrich the conformational ensembles of IDPs with specific features for adapting to changing molecular and cellular environments.
This article was published in the following journal.
Name: Journal of molecular biology
Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered ...
NUPR1 is a protumoral multifunctional intrinsically disordered protein, which is activated during the acute phases of pancreatitis, interacting with several biomolecules through residues around Ala33 ...
Intrinsically disordered proteins (IDPs) are crucial players in various cellular activities. Several experimental and computational analyses have been conducted to study structural pliability and func...
Intrinsic disorder is more abundant in eukaryotic than prokaryotic proteins. Methods predicting intrinsic disorder are based on the amino acid sequence of a protein. Therefore, there must exist an und...
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The evaluation of protein quality has been identified as the top priority question by the Food and Agricultural Organization (FAO) of the United Nations. However, the current available met...
Proline is a non-essential amino acid that helps with collagen formation. Collagen is one of the main ingredients of skin, bone, tendons, and connective tissue. It is thought that proline ...
The purpose of this study is to test whether Varenicline can help ambivalent smokers (those who are interested in quitting at some point in the future but have no current plans to quit) to...
The objective of this study is to assess the efficacy, tolerability, safety and pharmacokinetics of IgG with Proline (IgPro) in subjects with PID. The study should evaluate whether the ra...
The study was performed to investigate the effects of the consumption of black currant seed press residues, which were baked into bread.
Functional proteins that do not have unique, stable, folded, three-dimensional native structures or that possess non-ordered regions under physiological conditions. They are characterized by extraordinary structural flexibility and plasticity, which enable them to adopt different conformations in response to different stimuli or different interactions.
Protein domains that are enriched in PROLINE. The cyclical nature of proline causes the peptide bonds it forms to have a limited degree of conformational mobility. Therefore the presence of multiple prolines in close proximity to each other can convey a distinct conformational arrangement to a peptide chain.
A family of low molcular-weight proteins that contain PROLINE-RICH PROTEIN DOMAINS. Members of this family play a role in the formation of an insoluble cornified envelope beneath the plasma membrane of stratified squamous epithelial cells.
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
An approximately 40 amino acid protein domain that occurs in a variety of unrelated proteins and may be repeated up to four times in some proteins. It is characterized by two TRYPTOHAN residues (WW) about 20 amino acids apart and folds into a stable triple-stranded BETA-SHEET. It binds PROLINE-RICH PROTEIN DOMAINS and PHOSPHOSERINE or PHOSPHOTHREONINE-containing protein domains that occur in many signal transducing and cytoskeletal proteins, such as DYSTROPHIN.
Biological therapy involves the use of living organisms, substances derived from living organisms, or laboratory-produced versions of such substances to treat disease. Some biological therapies for cancer use vaccines or bacteria to stimulate the body&rs...