Secondary Structure

Secondary structure in proteins consists of local inter-residue interactions mediated by hydrogen bonds. The most common secondary structures are alpha helices and beta sheets.
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Secondary Structure
Most proteins contain one or more stretches of amino acids that take on a characteristic structure in 3-D space. The most common of these are the alpha helix and the beta conformation.
Alpha Helix ...
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Secondary structure
A representation of the 3D structure of the Myoglobin protein. alpha helices are shown in colour, and random coil in white, there are no beta sheets in shown.
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secondary structure The structure of a protein created by the formation of hydrogen bonds between different amino acids; can be a pleated sheet, alpha helix, or random coil. Shape of a protein caused by attraction between R-groups of amino acids.
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secondary structure
The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between peptide linkages.
secondary succession ...
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secondary structure - the folded, coiled, or twisted shape of a polypeptide that results from hydrogen bonding between parts of a molecule. There are two types of secondary structure: alpha helix and a beta pleated sheet.
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Secondary structure
The oxygen or nitrogen atoms of the peptide bond are capable of hydrogen- bonding with hydrogen atoms elsewhere on the molecule.
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Secondary Structure: (also see Primary and Tertiary Structure) Local structure within a protein which is conferred by the nature of the side chains of adjacent amino acids (e.g., alpha helix, beta sheet, random coil); ...
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The secondary structure [of a protein] is comprised of signature folds that proteins typically take up: typically seen are things like alpha-helices, which look like corkscrews.
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: A planar secondary structure element of proteins. It is created by hydrogen bonding between the backbone atoms in two different polypeptide chains or segments of a single folded chain.
Bacillus
thuringiensis ...
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Contrast with intermediary metabolism secondary structure The localized conformation of a protein. sedimentation coefficient A physical constant specifying the rate of sedimentation of a particle in a centrifugal field under specified conditions.
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A regular element of secondary structure in proteins, in which two or more extended strands of the polypeptide chain lie side by side (running either parallel or antiparallel), ...
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beta- pleated sheet-A planar secondary structure element of proteins that is created by hydrogen bonding between the backbone atoms in two different polypeptide chains or segment of a single folded chain.
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Attenuator
A region of leader mRNA that can form alternative secondary structures that determine whether transcription is terminated or proceeds into downstream genes. See Attenuation.
Att site
See attachment site.
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This helical, usually right-handed arrangement of a polypeptide chain is a common secondary structure in proteins. The helix has maximal intra-chain hydrogen bonding.
Related Terms: Polypeptide ...
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When the secondary structure of apo-AIMilano was investigated by spectrofluoroscopy and circular dichroism, a higher fluorescence peak wavelength and a lower alpha-helical content were detected in the variant apoprotein compared to normal AI.
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Reverse genetics studies of several such RNAs identified a secondary structure element, dubbed the hammerhead as responsible for the self-cleavage of the RNA.
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alpha-helix Literally the first spiral arrangement of the genetic DNA molecule; regular coiled arrangement of polypeptide chain in proteins; secondary structure of proteins.
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