Structural Biology in Drug Discovery 2020
DOI: 10.1002/9781118681121.ch25
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Intrinsically Disordered Proteins

Abstract: Many functional proteins do not have well defined folded structures. In recent years, both experimental and computational approaches have been developed to study the conformational behaviour of this type of protein. It has been shown previously that experimental RDCs (residual dipolar couplings) can be used to study the backbone sampling of disordered proteins in some detail. In these studies, the backbone structure was modelled using a common geometry for all amino acids. In the present paper, we demonstrate … Show more

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Cited by 17 publications
(22 citation statements)
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“…The existence of IDPs/IDPRs was established based on non-existing electron density of some regions in proteins during crystallography [12,46]. This unmapped electron density of characterized protein was later described as intrinsic disorderness of proteins.…”
Section: Spike Cytoplasmic Region Shows No Change In Presence Of Macromolecular Crowdersmentioning
confidence: 99%
See 1 more Smart Citation
“…The existence of IDPs/IDPRs was established based on non-existing electron density of some regions in proteins during crystallography [12,46]. This unmapped electron density of characterized protein was later described as intrinsic disorderness of proteins.…”
Section: Spike Cytoplasmic Region Shows No Change In Presence Of Macromolecular Crowdersmentioning
confidence: 99%
“…Generally, intrinsically disordered proteins show such characteristic of missing electron density and lacks a well-defined three-dimensional structure [12]. Additionally, the consensus-based disorder prediction by MobiDB has shown this region to be disordered [13].…”
Section: Graphical Abstract: Introductionmentioning
confidence: 99%
“…Despite of availability of several structures of spike protein using advanced techniques like cryo-EM, the structure of cytoplasmic domain is not yet clear due to its ‘missing electron density’. Generally, intrinsically disordered proteins show such characteristic of missing electron density and lacks a well-defined three-dimensional structure ( Uversky, 2020 ). Additionally, the consensus-based disorder prediction by MobiDB has shown this region to be disordered ( Piovesan et al, 2021 ).…”
Section: Introductionmentioning
confidence: 99%
“…Many IDPs gain secondary structure when binding onto surfaces, for example, to a cell membrane [ 2 ]. Since IDPs/IDRs cannot fold spontaneously and some of them require partners to acquire a more ordered structure, these proteins do not have a code that defines the capacity of foldable proteins to fold spontaneously into a biologically active structure [ 4 ]. A typical IDP/IDR has a multitude of elements for potentially foldable, partially foldable, differently foldable, or unfoldable protein segments [ 5 , 6 ].…”
Section: Introductionmentioning
confidence: 99%
“…Recent advances in heteronuclear multidimensional nuclear magnetic resonance (NMR) have allowed the complete assignment of resonances for several IDPs. NMR can also provide data about mobility of the unstructured regions [ 4 , 11 ]. In this way, NMR is possibly the most powerful technique for structural studies of these disordered proteins [ 12 ].…”
Section: Introductionmentioning
confidence: 99%