A number of different domain types interact with histone tails to read, write or erase
protein side chain modifications.
DNA sequence discrimination by CAP derives both from sequence - dependent distortion of the DNA helix and from direct hydrogen - bonding interactions between three
protein side chains and the exposed edges of three base pairs in the major groove of the DNA.
Not exact matches
The amino acid backbones snap together like beads on a string, the
side chains arranged in a particular order for each
protein.
And like
protein structures, the TZP
side chains were arranged in specific positions around the exterior of the rods formed by the backbone - backbone interactions.
Grate needed three things to mimic
proteins: raw components with a backbone that can support a large variety of
side chains; the ability to put the
side chains in a particular order; the stickiness, which chemists refer to as non-covalent bonds.
Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no
protein side -
chain atoms closer than about 18 angstroms to the peptide bond being synthesized.
Using their innovative approach, Emsley's team found that the sequence of
protein motions follows a specific hierarchy as temperature increases: first the
protein's solvent molecules, then the
protein's
side -
chains and water molecules, and finally the
protein's backbone.
In a
protein the cogs and springs are the molecules that make it up: amino acids form its backbone each with
side -
chains of different molecules branching out on all
sides in three dimensions.
Depending on the properties of the peaks on the diagram, scientists can determine the degree of motion of each atom in the
protein, e.g. its backbone, a
side -
chain etc..
In the new study, the researchers were able to determine that the water molecules directly touched the
protein's «
side chains,» the portions of the
protein molecule that bind and unbind with each other to enable folding and function.
Images produced by the study clearly show the structure of the proteasome complex — with the
protein backbone of each of its 28 subunits visible along with most of the
side chains of the
proteins.
To do so, they added back a small amount of the NOE and RDC data, but just in the parts of the analysis that deduce the shape of the general backbone of the
protein rather then the position of all the individual atoms in each amino acid
side chain.
They then relied on their ROSETTA software to sort out the position of the atoms in the
protein's
side chains.
In this case, the handholds are the amino acid
side chains of a
protein that will interact with other
proteins or small molecules, and the body is the folding of the
protein that incorporates all the amino acids into one structure.
The Meiler laboratory leads the further development of ROSETTALIGAND (Meiler, J.; Baker, D. «ROSETTALIGAND:
Protein - small molecule docking with full
side -
chain flexibility»;
Proteins 2006; 65; 538 - 548).
SUMO ligases conjugate the
protein, via its C - terminal carboxylate, to the
side -
chain lysine of target
proteins to generate an isopeptide linkage.
Amongst the 22 amino acids vital for our body to function and manufacture
proteins, glycine is the smallest and simplest, with only a single hydrogen forming its
side chain.
The
side chain of the molecule connects to the
protein backbone at two points.
So, the difference in plant and animal - based foods must be either due to a lower percentage of
protein, which might reduce IGF - 1 production, or due to some accompanying factor in the food such as sterols in animal products vs. phytosterols in plants, which have a different chemical structure such as their extra ethyl group on their
side -
chain.