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A random-coil conformation can be detected using spectroscopic techniques. The arrangement of the planar amide bonds results in a distinctive signal in circular dichroism. The chemical shift of amino acids in a random-coil conformation is well known in nuclear magnetic resonance (NMR). Deviations from these signatures often indicates the ...
Figure 1: The classic example of a coiled coil is the GCN4 leucine zipper (PDB accession code 1zik), which is a parallel, left-handed homodimer. However, many other types of coiled coil exist. A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands
The standard hydrogen-bond definition for secondary structure is that of DSSP, which is a purely electrostatic model. It assigns charges of ±q 1 ≈ 0.42e to the carbonyl carbon and oxygen, respectively, and charges of ±q 2 ≈ 0.20e to the amide hydrogen and nitrogen, respectively. The electrostatic energy is
Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]
Magnetotaxis is a process implemented by a diverse group of Gram-negative bacteria that involves orienting and coordinating movement in response to Earth's magnetic field. [1] This process is mainly carried out by microaerophilic and anaerobic bacteria found in aquatic environments such as salt marshes, seawater, and freshwater lakes. [ 2 ]
Simple hydrolysis will split the polypeptide chain, where the displaced amino group becomes the new N-terminus. This is seen in the maturation of glycosylasparaginase. A β-elimination reaction also splits the chain, but results in a pyruvoyl group at the new N-terminus.
1. The recognition of codons by release factors, which causes the hydrolysis of the polypeptide chain from the tRNA located in the P site [1] 2. The release of the polypeptide chain [57] 3. The dissociation and "recycling" of the ribosome for future translation processes [57] A summary table of the key players in translation is found below:
Three-dimensional structure [1] of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is ...