According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?

Dyson, H. Jane; Wright, Peter E.

doi:10.1080/15216540500484376

Cited by 20 publications

(15 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although the importance of intrinsically disordered proteins is established and will continue to grow, especially in the fields of evolution and drug design, it is yet to reach the textbook level and ultimate recognition. Indeed, current biochemistry textbooks ignore disordered proteins (206), and in our view, this omission has serious consequences, leading to a significant retardation in the understanding of protein structure/function relationships.…”

Section: Discussionmentioning

confidence: 99%

Intrinsic Disorder and Functional Proteomics

Radivojac

Iakoucheva

Oldfield

et al. 2007

Biophysical Journal

654

586

View full text Add to dashboard Cite

The recent advances in the prediction of intrinsically disordered proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed here, especially with regard to protein function. First, a close look is taken at intrinsically disordered proteins and then at the methods used for their experimental characterization. Next, the major statistical properties of disordered regions are summarized, and prediction models developed thus far are described, including their numerous applications in functional proteomics. The future of the prediction of protein disorder and the future uses of such predictions in functional proteomics comprise the last section of this article.

show abstract

Section: Discussionmentioning

confidence: 99%

Intrinsic Disorder and Functional Proteomics

Radivojac

Iakoucheva

Oldfield

et al. 2007

Biophysical Journal

654

586

View full text Add to dashboard Cite

show abstract

“…All known forms of MBP (both classic and Golli) belong to the emerging class of “intrinsically disordered” proteins (IDPs), which have also been referred to as “intrinsically unstructured,” “natively unstructured,” or “conformationally adaptable” (Fig. 2) (Harauz et al, 2004; Dyson and Wright, 2006; Receveur‐Bréchot et al, 2006). Many IDPs are involved in signalling pathways and have been identified to be multifunctional.…”

Section: Physicochemical Properties Of Murine Bg21mentioning

confidence: 99%

Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein

Bamm

Ahmed

Ladizhansky

et al. 2006

J of Neuroscience Research

View full text Add to dashboard Cite

A recombinant form of the murine Golli-myelin basic protein (MBP) isoform BG21 (rmBG21) has been expressed in E. coli, and isolated to 96% purity via metal chelation chromatography. Characteristic yields were 6-8 mg protein per liter of culture in either minimal M9 or standard Luria-Bertani media. Circular dichroism spectroscopy showed that rmBG21 had a large proportion of random coil in aqueous solution, but gained alpha-helix in the presence of monosialoganglioside G(M1) and PI(4)P, as well as in the membrane-mimetic solvent trifluoroethanol. Bioinformatics analyses of the amino acid sequence of rmBG21 predicted an N-terminal calmodulin (CaM)-binding site. It was determined by fluorescence spectroscopy and dynamic light scattering that rmBG21 and CaM interacted weakly in a 1:1 ratio in a Ca(2+)-dependent manner. Solution NMR spectra of uniformly [(13)C(15)N]-labeled protein in aqueous buffer were consistent with it being an extended protein; spectral quality was independent of temperature. Thus, like "classic" MBP and the Golli-MBP isoform J37, rmBG21 is intrinsically disordered, implying multi functionality, and that its conformation depends on its environment and bound ligands.

show abstract

“…Bio-NMR, previously best known for the structural determination of small globular proteins, has now imposed itself as a method of choice in the emerging field of unstructured protein biochemistry [5]. NMR spectroscopy is still in a phase of fast technological advances, with increased magnetic fields allowing for better resolution and sensitivity, and novel probe heads allowing for smaller volumes to be analysed with good signal to noise ratios.…”

Section: Nmr Spectroscopy Of the Tau Proteinmentioning

confidence: 99%

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease

Landrieu

Leroy

Smet‐Nocca

et al. 2010

Biochemical Society Transactions

View full text Add to dashboard Cite

NMR spectroscopy was used to explore the different aspects of the normal and pathological functions of tau, but proved challenging because the protein contains 441 amino acids and has poor signal dispersion. We have set out to dissect the phosphorylation patterns of tau in order to understand better its role in the aggregation process and microtubule-binding regulation. Our current knowledge on the functional consequences of specific phosphorylations is still limited, mainly because producing and assessing quantitatively phosphorylated tau samples is far from straightforward, even in vitro. We use NMR spectroscopy as a proteomics tool to characterize the phosphorylation patterns of tau, after in vitro phosphorylation by recombinant kinases. The phosphorylated tau can next be use for functional assays or interaction assays with phospho-dependent protein partners, such as the prolyl cis-trans isomerase Pin1.

show abstract

According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?

Cited by 20 publications

References 34 publications

Intrinsic Disorder and Functional Proteomics

Intrinsic Disorder and Functional Proteomics

Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease

Contact Info

Product

Resources

About