# Intrinsically Disordered Protein
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In 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.
IDPs are a very large and functionally important class of proteins.
Intrinsically Disordered Proteins with Professor Priyanka Joshi, Ph.D.
Unlike “globular” proteins that adopt stable structures that are relatively easy to analyze, intrinsically disordered proteins adopt many context-dependent shapes. These shapes may drive diverse functions, but they are also difficult to capture and study. This represents a large gap in our unders...
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A New Era In Alzheimer's Research with Sarah DeVos
Do you have a question you'd like answered on a future episode of Translating Proteomics? Send it to translatingproteomics@nautilus.bio!
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NSP 11 of SARS-CoV-2 is an Intrinsically Disordered Protein
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2020.10.07.330068v1?rss=1
Authors: Gadhave, K., Kumar, P., Kumar, A., Bhardwaj, T., Garg, N., Giri, R.
Abstract:
The intrinsically disordered proteins/regions (IDPs/IDPRs) are known to be responsible for multiple cellular processes a...
Intrinsically disordered protein ensembles shape evolutionary rates revealing conformational patterns
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2020.07.29.227363v1?rss=1
Authors: Palopoli, N., Marchetti, J., Monzon, A. M., Zea, D. J., Tosatto, S. C. E., Fornasari, M. S., Parisi, G.
Abstract:
Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physio...
The intrinsically disordered protein SPE-18 promotes localized assembly of the major sperm protein in C. elegans spermatocytes
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2020.08.10.244988v1?rss=1
Authors: Price, K. L., Presler, M., Uyehara, C., Shakes, D.
Abstract:
Many specialized cells use unconventional strategies of cytoskeletal control. Nematode spermatocytes discard their actin and tubulin foll...
Histidine-rich Ca2+-binding protein stimulates the transport cycle of SERCA through a conformation-dependent fuzzy complex.
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2020.09.17.302869v1?rss=1
Authors: Ayeotan, T. I., Hansen, L. C., Boesen, T., Olesen, C. E., Moeller, J. V., Nissen, P., Kjaergaard, M.
Abstract:
The histidine-rich Ca2+-binding protein (HRC) stimulates the sarco-endoplasmic reticulu...
α-Synuclein facilitates endocytosis by elevating the steady-state levels of phosphatidylinositol 4,5-bisphosphate
Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2020.06.18.158709v1?rss=1
Authors: Schechter, M., Atias, M., Abd Elhadi, S., Davidi, D., Gitler, D., Sharon, R.
Abstract:
alpha-Synuclein (a-Syn) is a protein implicated in the pathogenesis of Parkinson s disease (PD). It is an intri...
Antoine Gruet and David Blocquel
Fuzzy regions in an intrinsically disordered protein impair protein–protein interactions
Creating new and better medicines, featuring Virginia Burger of New Equilibrium Biosciences
In one sentence...
Computational biology is enhancing our understanding of intrinsically disordered proteins, leading to exciting new medical treatments.
Overview
From videogames to protein discovery, high performance computing impacts how we understand and engage with each other and the world ar...
