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Turn (biochemistry)

Index Turn (biochemistry)

A turn is an element of secondary structure in proteins where the polypeptide chain reverses its overall direction. [1]

17 relations: Allosteric regulation, Amino acid, Beta bend ribbon, Beta hairpin, Beta turn, Biomolecular structure, Chirality, Conformational change, Dihedral angle, Enantiomer, Gajendra Pal Singh Raghava, Hydrogen bond, Intrinsically disordered proteins, Peptide bond, Proline, Protein folding, Ramachandran plot.

Allosteric regulation

In biochemistry, allosteric regulation (or allosteric control) is the regulation of an enzyme by binding an effector molecule at a site other than the enzyme's active site.

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Amino acid

Amino acids are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.

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Beta bend ribbon

The beta bend ribbon, or beta-bend ribbon, is a structural feature in polypeptides and proteins.

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Beta hairpin

The beta hairpin (sometimes also called beta-ribbon or beta-beta unit) is a simple protein structural motif involving two beta strands that look like a hairpin.

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Beta turn

A β turn is a type of non-regular secondary structure in proteins that causes a change in direction of the polypeptide chain.

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Biomolecular structure

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.

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Chirality

Chirality is a property of asymmetry important in several branches of science.

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Conformational change

In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.

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Dihedral angle

A dihedral angle is the angle between two intersecting planes.

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Enantiomer

In chemistry, an enantiomer, also known as an optical isomer (and archaically termed antipode or optical antipode), is one of two stereoisomers that are mirror images of each other that are non-superposable (not identical), much as one's left and right hands are the same except for being reversed along one axis (the hands cannot be made to appear identical simply by reorientation).

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Gajendra Pal Singh Raghava

Gajendra Pal Singh Raghava is an Indian bio-informatician and head of Comutational Biology at the Indraprastha Institute of Information Technology (IIIT), Delhi.

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Hydrogen bond

A hydrogen bond is a partially electrostatic attraction between a hydrogen (H) which is bound to a more electronegative atom such as nitrogen (N), oxygen (O), or fluorine (F), and another adjacent atom bearing a lone pair of electrons.

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Intrinsically disordered proteins

An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure.

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Peptide bond

A peptide bond is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain.

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Proline

Proline (symbol Pro or P) is a proteinogenic amino acid that is used in the biosynthesis of proteins.

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Protein folding

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.

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Ramachandran plot

A Ramachandran plot (also known as a Ramachandran diagram or a plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino acid residues in protein structure.

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Redirects here:

Beta-turn, Gamma turn, Loop (biochemistry).

References

[1] https://en.wikipedia.org/wiki/Turn_(biochemistry)

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