How Do You Spell CHAPERONIN FAMILY?

Pronunciation: [ʃˈapəɹˌə͡ʊnɪn fˈamɪli] (IPA)

The spelling of "Chaperonin Family" may seem like a challenge, but it becomes clearer with the use of IPA phonetic transcription. The first syllable, "cha," is pronounced as /ʃɑ:/ or "shah," followed by "pe," pronounced as /pɛ/ or "peh." The next syllable is "ro," pronounced as /ro/ or "row," and "nin" is pronounced as /nɪn/ or "nin." The final two syllables, "Family," are pronounced as /ˈfæm.ə.li/ or "fam-uh-lee." Thus, using IPA phonetics can aid in the understanding and pronunciation of challenging terms like "Chaperonin Family."

CHAPERONIN FAMILY Meaning and Definition

1. The chaperonin family refers to a diverse group of proteins that play a vital role in folding and refolding unfolded or misfolded proteins within cells. Chaperonins are ubiquitous and present in various organisms, including bacteria, archaea, and eukaryotes. They are typically large, multi-subunit protein complexes that provide a protected environment for protein folding or refolding.

   The primary function of chaperonins is to prevent the aggregation and aggregation-prone intermediates of proteins, facilitating their proper folding into their native three-dimensional structures. They act as molecular chaperones, assisting in overcoming the complexities of protein folding by providing a suitable environment that allows for efficient and accurate folding.

   The chaperonin family is characterized by its conserved structural and functional features. Its central structural motif is a large, double-ring structure enclosing a central cavity. This structure provides the essential folding chamber within which the unfolded or misfolded protein can be encapsulated.

   The chaperonin family is made up of several subgroups, including the well-known eukaryotic group called Chaperonin Containing TCP-1 (CCT), which is involved in folding cytosolic proteins. Other subfamilies include GroEL/GroES in bacteria and archaea, which are crucial for protein folding within the bacterial cytoplasm, as well as thermosome and HSP60 in archaea and mitochondria, respectively.

   In summary, the chaperonin family comprises a diverse set of proteins that act as molecular chaperones, assisting in the folding and refolding of proteins. They provide a protected environment to ensure proper folding and prevent protein aggregation, thereby maintaining cellular functionality.

Common Misspellings for CHAPERONIN FAMILY

• xhaperonin family
• vhaperonin family
• fhaperonin family
• dhaperonin family
• cgaperonin family
• cbaperonin family
• cnaperonin family
• cjaperonin family
• cuaperonin family
• cyaperonin family
• chzperonin family
• chsperonin family
• chwperonin family
• chqperonin family
• chaoeronin family
• chaleronin family
• cha-eronin family
• cha0eronin family
• chapwronin family
• chapsronin family

Etymology of CHAPERONIN FAMILY

The word "chaperonin" comes from the French word "chaperon", which means "hood" or "cap". It was originally used in reference to a woman's hooded cloak, which later developed into the sense of a guide or protector. The term "chaperonin" was coined in 1980 to describe a class of proteins that act as molecular chaperones, guiding the folding or assembly of other proteins. The addition of "family" in "chaperonin family" implies a group of related proteins that exhibit similar functions as molecular chaperones.