Globular protein: Difference between revisions
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Globular proteins are one of two types of proteins, the other being [[Fibrous protein|Fibrous proteins]]. Globular proteins have a compact and relatively spherical structure. Globular proteins are soluble in water and tend to be involved in metabolic functions, as opposed to fibrous proteins which tend to have a structural role. The [[Polypeptide|polypeptide]] chain of a globular protein can be folded into regions of α-helical or β-sheet structures forming the secondary structure of the protein. The secondary structure can be majoritively α-helical, majoritively β-sheet or a combination of both the structures. These [[Secondary structure|sec]][[Secondary structure|ondary structures]] are then folded on one another to form the globular [[Tertiary structure|tertiary structure]] of the protein. The α-helix and β-sheet regions contain random coils forming irregular structured regions which allow for the polypeptide chain to fold in a unique way. This means that every globular protein has a unique tertiary structure which is specific to the function of that protein. | Globular proteins are one of two types of proteins, the other being [[Fibrous protein|Fibrous proteins]]. Globular proteins have a compact and relatively spherical structure. Globular proteins are soluble in water and tend to be involved in metabolic functions, as opposed to fibrous proteins which tend to have a structural role. The [[Polypeptide|polypeptide]] chain of a globular protein can be folded into regions of α-helical or β-sheet structures forming the secondary structure of the protein. The secondary structure can be majoritively α-helical, majoritively β-sheet or a combination of both the structures. These [[Secondary structure|sec]][[Secondary structure|ondary structures]] are then folded on one another to form the globular [[Tertiary structure|tertiary structure]] of the protein. The [[Alpha-helix|α-helix]] and [[Beta-sheet|β-sheet ]]regions contain random coils forming irregular structured regions which allow for the [[Polypeptide|polypeptide]] chain to fold in a unique way. This means that every globular protein has a unique tertiary structure which is specific to the function of that protein. | ||
Common globular proteins include [[Haemoglobin|haemoglobin]], [[Myoglobin|myoglobin]], [[Immunoglobulin|immunoglobin]] and [[Insulin|insulin]]<ref>Hardin, J, Bertoni, G and Kleinsmith, LJ 2012, Becker's World of the Cell, 8th edn, Pearson Bejamin Cummings. p.51</ref>. | Common globular proteins include [[Haemoglobin|haemoglobin]], [[Myoglobin|myoglobin]], [[Immunoglobulin|immunoglobin]] and [[Insulin|insulin]]<ref>Hardin, J, Bertoni, G and Kleinsmith, LJ 2012, Becker's World of the Cell, 8th edn, Pearson Bejamin Cummings. p.51</ref>. | ||
Latest revision as of 14:37, 9 December 2018
Globular proteins are one of two types of proteins, the other being Fibrous proteins. Globular proteins have a compact and relatively spherical structure. Globular proteins are soluble in water and tend to be involved in metabolic functions, as opposed to fibrous proteins which tend to have a structural role. The polypeptide chain of a globular protein can be folded into regions of α-helical or β-sheet structures forming the secondary structure of the protein. The secondary structure can be majoritively α-helical, majoritively β-sheet or a combination of both the structures. These secondary structures are then folded on one another to form the globular tertiary structure of the protein. The α-helix and β-sheet regions contain random coils forming irregular structured regions which allow for the polypeptide chain to fold in a unique way. This means that every globular protein has a unique tertiary structure which is specific to the function of that protein.
Common globular proteins include haemoglobin, myoglobin, immunoglobin and insulin[1].
References
- ↑ Hardin, J, Bertoni, G and Kleinsmith, LJ 2012, Becker's World of the Cell, 8th edn, Pearson Bejamin Cummings. p.51