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What is histidine hydrochloride?
Histidine hydrochloride is a salt form of the amino acid histidine. It is commonly used in biochemical studies and in cell culture media as a source of histidine. Histidine is an essential amino acid that plays a role in protein synthesis and is important for various metabolic processes in the body.
When was the chemical compound histidine first discovered?
The chemical compound Histidine was first discovered in 1896. Histidine was discovered by German phsician Albercht Kossel. Histidine can be found in all human beings.
Why histidine is often found at the active-site of enzyme?
Histidine can act as a versatile amino acid in enzyme active sites because of its ability to donate and accept protons over a wide pH range. This allows histidine to participate in various catalytic mechanisms, making it a common residue in enzyme active sites. Additionally, the imidazole side chain of histidine can form hydrogen bonds and coordinate with metal ions, further enhancing its role in enzyme catalysis.
First part of bowel distal to the stomach?
The first part of the bowel distal to the stomach is the duodenum. It is the shortest and widest part of the small intestine and plays a critical role in the absorption of nutrients.
What is a distal clavi?
A distal clavi is a bone, also known as the clavicle or collarbone, located in the body that connects the shoulder blade to the sternum. It plays a crucial role in stabilizing and supporting the shoulder joint.
Why myoglobin has high affinity to oxygen?
Myoglobin has a high affinity for oxygen due to the heme group present within its structure, which can form strong bonds with oxygen molecules. The heme group has a distal histidine residue that stabilizes the bound oxygen molecule, contributing to the high affinity of myoglobin for oxygen. Additionally, myoglobin has a hydrophobic pocket that further enhances its ability to bind oxygen tightly.
What is histidine hydrochloride?
Histidine hydrochloride is a salt form of the amino acid histidine. It is commonly used in biochemical studies and in cell culture media as a source of histidine. Histidine is an essential amino acid that plays a role in protein synthesis and is important for various metabolic processes in the body.
What type of proteins require a covalent bonded prosthetic group to function properly?
Proteins such as haemoglobin and myoglobin which require haem groups covalently bonded to the proximal histidine (HisF8) residue for O2 binding.
What does myoglobin do for muscles?
Myoglobin's function is similar to that of hemoglobin, which carries oxygen in red blood cells to various tissues. Myoglobin has even higher affinity for oxygen than hemoglobin and is specific to muscle cells. Myoglobin thus acts as a storage of oxygen, as it holds oxygen inside heart and skeletal muscles.
Is myoglobin an enzyme?
No, myoglobin is not an enzyme. It is a protein that is responsible for binding and storing oxygen in muscle cells. Its main role is to facilitate the storage and release of oxygen to muscles during physical activity.
Which is most related to the role of myoglobin?
Myoglobin is primarily related to the storage and transport of oxygen in muscle tissues. It binds oxygen molecules more tightly than hemoglobin, allowing for efficient oxygen supply during muscle contraction. Additionally, myoglobin plays a crucial role in muscle metabolism, especially in endurance activities, by facilitating oxygen availability to support aerobic respiration.
When was the chemical compound histidine first discovered?
The chemical compound Histidine was first discovered in 1896. Histidine was discovered by German phsician Albercht Kossel. Histidine can be found in all human beings.
What codon is the code for the amino acid histidine His?
The mRNA codons for histidine are CAU and CAC.
What compound stored oxygen inside skeletal muscle cells?
keratinThe correct answer is NOT keratin... the correct answer is myoglobin. This is the oxygen-binding pigment in muscle.
What is the role of the Myoglobin?
Myoglobin is a protein found in muscle tissue of vertebrates that is iron- and oxygen-binding. It is a primary oxygen-carrying pigment of muscle tissues and is related to hemoglobin, but only found in the bloodstream after a muscle injury.
Is myoglobin and myoglobulin the same?
No, myoglobin and myoglobulin are not the same. Myoglobin is a protein found in muscle tissues that binds and stores oxygen, while myoglobulin is a misspelling or incorrect term for myoglobin.
Is myoglobin bad for you?
Myoglobin is a protein found in muscle tissues that binds and stores oxygen, playing a crucial role in muscle metabolism. It is not inherently bad for you; in fact, it is essential for muscle function. However, elevated levels of myoglobin in the bloodstream, often due to muscle injury, can lead to complications like kidney damage. Maintaining overall muscle health is important to ensure myoglobin levels remain within a normal range.
