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Journal ArticleDOI

Probing the conformational state of apomyoglobin by limited proteolysis.

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TLDR
It is shown here that limited proteolysis can probe the structural and dynamic differences between the holo and apo form of horse myoglobin and is a useful and reliable method for probing structure and dynamics of proteins, complementing other experimental techniques such as NMR and X-ray crystallography.
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This article is published in Journal of Molecular Biology.The article was published on 1997-02-21. It has received 201 citations till now. The article focuses on the topics: Proteolytic enzymes & Proteolysis.

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Intrinsically Disordered Proteins

TL;DR: The sequence-structure relationships indicate that disorder is an encoded property, and the predictions strongly suggest that proteins in nature are much richer in intrinsic disorder than are those in the Protein Data Bank.
Journal ArticleDOI

The importance of intrinsic disorder for protein phosphorylation

TL;DR: A new web-based tool for the prediction of protein phosphorylation sites, DISPHOS (DISorder-enhanced PHOSphorylation predictor, http://www.ist. edu/DISPHOS), which observes that amino acid compositions, sequence complexity, hydrophobicity, charge and other sequence attributes of regions adjacent to phosphate sites are very similar to those of intrinsically disordered protein regions.
Journal ArticleDOI

Understanding protein non-folding.

TL;DR: This review describes the family of intrinsically disordered proteins, members of which fail to form rigid 3-D structures under physiological conditions, either along their entire lengths or only in localized regions.
Journal ArticleDOI

Intrinsically disordered proteins and intrinsically disordered protein regions.

TL;DR: This work presents several early examples and the mechanisms by which IDPs contribute to function, which it hopes will encourage comprehensive discussion of IDPs and IDP regions in biochemistry textbooks and propose future directions for IDP research.
Journal ArticleDOI

Probing protein structure by limited proteolysis.

TL;DR: The results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.
References
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Journal ArticleDOI

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.
Journal ArticleDOI

The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites

TL;DR: In this paper, anilino-8-naphthalene sulfonate (ANS) was used as a fluorescent probe of non-polar regions in proteins and its fluorescence changes markedly when it is bound to the apoprotein.
Book

Proteolytic enzymes : a practical approach

TL;DR: P.H. North: Prevention of unwanted proteolysis V.V.C. Price: Proteinase as probes of conformation J.M. Pratt: Proteases as membrane probes P.E. Butler: Solubilization of membrane proteins P.B. Neurath: The diversity of proteolytic enzymes G. DeMartino, R.S. Sarath, & F. Wagner : Proteax assay methods.
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