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Copied from CapZ

Every fact is labeled with a reference. Every reference link works and leads to an appropriate references. One of the references provided is from 2003, which I consider outdated because science is making progress every year. The information used in this article come from reliable sources such as journals. The section on cardiac health was underrepresented. There is only one sentence on the subject. It could be helpful if there was or information on health issues, if any, that occur due to a mutation of CapZ protein. Another topic that could have been in the article page is in regards to the structure. CapZ is a protein, which means it is made of amino acids and depending on which amino acids, CapZ could have certain unique properties. The article itself is neutral. Aside from the mentioned edits, the article gives good reliable information.

Structure

CapZ is a heterodimeric molecule, made up of an α and β subunit. The α and β subunits are similar in structure. Each subunit is divided into three domains and a shared C-terminal extension. Helix 1-3 is an N-terminal that is composed of three antiparallel helices that are arranged in an up, down, up pattern. Helix 4 is a C-terminal made up of an antiparallel β sheet which is composed of five β strands. On one side of the C-terminal, there is a shorter N-terminal helix and a long C-terminal helix. This long C-terminal helix makes up helix 5. The final helix, helix 6 differs in the α and β subunits. The β subunit is longer than the α subunit.