About: (13)C Chemical Shifts in Proteins: A Rich Source of Encoded Structural Information

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	(13)C Chemical Shifts in Proteins: A Rich Source of Encoded Structural Information
Creator	Vila, J Vila, Jorge Arnautova, Y Arnautova, Yelena
Source	PMC
abstract	Despite the formidable progress in Nuclear Magnetic Resonance (NMR) spectroscopy, quality assessment of NMR-derived structures remains as an important problem. Thus, validation of protein structures is essential for the spectroscopists, since it could enable them to detect structural flaws and potentially guide their efforts in further refinement. Moreover, availability of accurate and efficient validation tools would help molecular biologists and computational chemists to evaluate quality of available experimental structures and to select a protein model which is the most suitable for a given scientific problem. The (13)C(α) nuclei are ubiquitous in proteins, moreover, their shieldings are easily obtainable from NMR experiments and represent a rich source of encoded structural information that makes (13)C(α) chemical shifts an attractive candidate for use in computational methods aimed at determination and validation of protein structures. In this chapter, the basis of a novel methodology of computing, at the quantum chemical level of theory, the (13)C(α) shielding for the amino acid residues in proteins is described. We also identify and examine the main factors affecting the (13)C(α)-shielding computation. Finally, we illustrate how the information encoded in the (13)C chemical shifts can be used for a number of applications, viz., from protein structure prediction of both α-helical and β-sheet conformations, to determination of the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH or to accurate detection of structural flaws, at a residue-level, in NMR-determined protein models.
has issue date	2018-07-20(xsd:dateTime)
bibo:doi	10.1007/978-3-319-95843-9_20
has license	no-cc
sha1sum (hex)	4604720c02a58dd3687f0897f7204cba47665108
schema:url	https://doi.org/10.1007/978-3-319-95843-9_20
resource representing a document's title	(13)C Chemical Shifts in Proteins: A Rich Source of Encoded Structural Information
has PubMed Central identifier	PMC7123919
schema:publication	Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes
resource representing a document's body	covid:4604720c02a58dd3687f0897f7204cba47665108#body_text
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