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 ...
Secondary structure
From Wikipedia, the free encyclopedia
Jump to: navigation, search ...
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.
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 ...
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.
Secondary structure
The oxygen or nitrogen atoms of the peptide bond are capable of hydrogen- bonding with hydrogen atoms elsewhere on the molecule.
Secondary structure In a protein, the spatial arrangement of amino acid residues that are relatively close to one another in the linear sequence; the α helix and the β strand are both elements of primary structure.
Secondary Structure: The Alpha Helix ... The alpha helix was initially described in 1951 by Linus Pauling and Robert ... suppose the alpha helix is a preferred ...
Full article ...
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.
The secondary structure is the tendency of the polypeptide to coil or pleat due to H-bonding between R-groups. The tertiary structure is controlled by bonding (or in some cases repulsion) between R-groups.
The alpha helix and beta sheet are referred to as secondary structure (the bonds that maintain the secondary structure are hydrogen bonds). The 3-D shape of a protein is the result of it folding on itself.
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.
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
A long chain of amino acids joined by peptide bonds.
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.
Alpha helices and beta sheets are examples of secondary structure.
C.
Side chains (R-groups) of amino acids can be hydrophilic or hydrophobic.
Has strong influence on secondary structure of proteins and is much more abundant in collagens than in other proteins, occurring especially in the sequence glycine proline hydroxyproline.
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.
alpha-helix Literally the first spiral arrangement of the genetic DNA molecule; regular coiled arrangement of polypeptide chain in proteins; secondary structure of proteins.
 See also: Protein, Sequence, DNA, Trans, Proteins
|
