Publication

Relative Orientation of CaHa-Bond Vectors of Successive Residues in Proteins through Cross-Correlated Relaxation in NMR

Geoffrey Bodenhausen
2000
Journal Articles

Abstract

Cross-correlation between the fluctuations of 13Ca-Ha interactions affects the relaxation behavior of two-spin coherences (zero- and double-quantum coherences) involving the 13Ca nuclei of two successive amino acid residues. The cross-correlation rates are shown to depend on a dihedral angle S defined by two planes subtended by the atoms {Ha(i-1),13Ca(i-1),13Ca(i)} and {13Ca(i-1),13Ca(i),Ha(i)}. This dihedral angle is related to the secondary structure of a protein, and can be used as a constraint in various protein structure calcn. protocols. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/82554538-2d44-46d2-b0cb-dbc098d034c5

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Geoffrey Bodenhausen
2000
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/82554538-2d44-46d2-b0cb-dbc098d034c5

About this result

Related concepts (31)

Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Intraclass correlation

In statistics, the intraclass correlation, or the intraclass correlation coefficient (ICC), is a descriptive statistic that can be used when quantitative measurements are made on units that are organized into groups. It describes how strongly units in the same group resemble each other. While it is viewed as a type of correlation, unlike most other correlation measures, it operates on data structured as groups rather than data structured as paired observations.

Protein secondary structure

Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.

Related publications (10)

Relative Orientation of CaHa-Bond Vectors of Successive Residues in Proteins through Cross-Correlated Relaxation in NMR

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