Search results
Results from the WOW.Com Content Network
Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multi-protein complexes. [14] Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules ...
The polymerization of one kind of monomer gives a homopolymer. Many polymers are copolymers, meaning that they are derived from two different monomers. In the case of condensation polymerizations, the ratio of comonomers is usually 1:1. For example, the formation of many nylons requires equal amounts of a dicarboxylic acid and diamine. In the ...
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
[42]: 178–81 Some globular proteins can play structural functions, for example, actin and tubulin are globular and soluble as monomers, but polymerize to form long, stiff fibers that make up the cytoskeleton, which allows the cell to maintain its shape and size.
The quaternary structure of this protein complex would be described as a homo-trimer because it is composed of three identical smaller protein subunits (also designated as monomers or protomers). The number of subunits in an oligomeric complex is described using names that end in -mer (Greek for "part, subunit").
Structure of an example polyphenylene dendrimer macromolecule. [14] Some examples of macromolecules are synthetic polymers (plastics, synthetic fibers, and synthetic rubber), graphene, and carbon nanotubes. Polymers may be prepared from inorganic matter as well as for instance in inorganic polymers and geopolymers.
An example of a homo-oligomeric protein is collagen, which is composed of three identical protein chains. A tetrapeptide, a hetero-oligomer of the amino acids valine (green), glycine (black), serine (black), and alanine (blue).
In biochemistry, a protein dimer is a macromolecular complex or multimer formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di-+ -mer. A protein dimer is a type of protein quaternary structure.