Search results
Results From The WOW.Com Content Network
In protein structures, a beta barrel (β barrel) is a beta sheet (β sheet) composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand (hydrogen bond). Beta-strands in many beta-barrels are arranged in an antiparallel fashion.
The TIM barrel (triose-phosphate isomerase), also known as an alpha/beta barrel, [1]: 252 is a conserved protein fold consisting of eight alpha helices (α-helices) and eight parallel beta strands (β-strands) that alternate along the peptide backbone. [2] The structure is named after triose-phosphate isomerase, a conserved metabolic enzyme. [3]
An alpha/beta barrel is a protein fold formed by units composed of a short α-helix followed by two anti-parallel β-strands, followed by an α-helix and a β-strand; the three β-strands form a β-sheet that runs parallel to the barrel and the α-helix is in the outside of the barrel but does not contact the α-helices of the other repeats like in TIM barrels.
BamA is a β-barrel, outer membrane protein found in Gram-negative bacteria and it is the main and vital component of the β-barrel assembly machinery (BAM) complex in those bacteria. [1] BAM Complex consists of five components; BamB, BamC, BamD, BamE (all are lipoproteins ) and BamA (Outer membrane protein).
All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism. [7] In addition to the protein domains, there are unusual transmembrane elements formed by peptides. A typical example is gramicidin A, a peptide that forms a dimeric transmembrane β-helix ...
Porins are beta barrel proteins that cross a cellular membrane and act as a pore, through which molecules can diffuse. [1] Unlike other membrane transport proteins, porins are large enough to allow passive diffusion, i.e., they act as channels that are specific to different types of molecules.
The fold is an elaboration on the Greek key motif and is sometimes considered a form of beta barrel. It is very common in viral proteins, particularly viral capsid proteins. [3] [4] Taken together, the jelly roll and Greek key structures comprise around 30% of the all-beta proteins annotated in the Structural Classification of Proteins (SCOP ...
[6] [7] Neutron scattering measurements have directly connected the spectral feature at ~1 THz to collective motions of the secondary structure of beta-barrel protein GFP. [8] Hydrogen bonding patterns in secondary structures may be significantly distorted, which makes automatic determination of secondary structure difficult.