The spelling of the word "ef hand" can be explained using the International Phonetic Alphabet (IPA). The first part of the word, "ef," is spelled /ɛf/, as in the sound made by the letter F. The second part, "hand," is spelled /hænd/, with a silent H and the A pronounced as the short vowel sound. Together, the word is pronounced /ɛf hænd/. "Ef hand" refers to a specific type of protein domain found in many proteins involved in DNA recognition and binding.
The term "EF hand" refers to a structural motif or a protein domain found in a variety of calcium-binding proteins. It derives its name from the initials of the two pioneering researchers who first discovered this unique structure, Edgar R. Engleman and Stanley J. Fletterick. This motif is composed of approximately 30 amino acids and typically exists in pairs in a wide range of proteins.
The EF hand motif consists of a helix-loop-helix structure, with a calcium-binding loop in the center known as the EF loop. This loop contains a series of conserved acidic residues, often in the form of aspartate or glutamate, which directly coordinate the binding of calcium ions. When calcium ions are present, they bind to the EF loop, causing a conformational change in the protein, thereby regulating its function.
The EF hand motif is critical for mediating various biological processes, notably the regulation of calcium-dependent signaling pathways within cells. Many EF hand-containing proteins are involved in diverse physiological processes, such as muscle contraction, neuronal signaling, immune response, and gene expression. Examples of EF hand-containing proteins include calmodulin, troponin C, and S100 proteins.
In summary, the EF hand motif describes a unique calcium-binding structural motif present in various proteins. Its discovery has significantly contributed to our understanding of calcium signaling and its role in regulating numerous physiological processes.