Denaturation of proteins
... tertiary structure and, if applicable, quaternary structure) and how those forces would be affected by the changes in temperature or pH. For example, H bonds, such as in C=O∙∙∙∙H-N, are important in 2°, 3°, and 4° structure. As the temperature of a solution containing the protein is raised, the extr ...
... tertiary structure and, if applicable, quaternary structure) and how those forces would be affected by the changes in temperature or pH. For example, H bonds, such as in C=O∙∙∙∙H-N, are important in 2°, 3°, and 4° structure. As the temperature of a solution containing the protein is raised, the extr ...
1 Glycosylation and Protein Folding I. Introduction. As a translocated
... peptidase; 2) it is glycosylated; and 3) it must be helped to fold into the correct conformation. II. Signal peptidase. Cleavage of the signal peptide is carried out by the membrane enzyme, signal peptidase, that is associated with the Sec61 complex with its active site in the lumen of the ER. This ...
... peptidase; 2) it is glycosylated; and 3) it must be helped to fold into the correct conformation. II. Signal peptidase. Cleavage of the signal peptide is carried out by the membrane enzyme, signal peptidase, that is associated with the Sec61 complex with its active site in the lumen of the ER. This ...
Purified Sp1 protein
... gene expression in the early development of an organism. The protein is 785 amino acids long, with a molecular weight of 81 kDa. The SP1 transcription factor contains a zinc finger protein motif, by which it binds directly to DNA and enhances gene transcription. Its zinc fingers are of the Cys2/His2 ...
... gene expression in the early development of an organism. The protein is 785 amino acids long, with a molecular weight of 81 kDa. The SP1 transcription factor contains a zinc finger protein motif, by which it binds directly to DNA and enhances gene transcription. Its zinc fingers are of the Cys2/His2 ...
Force generation in dividing E
... opposite of what was aimed at occurs: the molecular handle is now present everywhere on the cell surface, except at the division site. In addition, Chapter 5 contains results on fusions between various other protein domains and OmpA-177. It seems that when protein domains are fused behind (C-termina ...
... opposite of what was aimed at occurs: the molecular handle is now present everywhere on the cell surface, except at the division site. In addition, Chapter 5 contains results on fusions between various other protein domains and OmpA-177. It seems that when protein domains are fused behind (C-termina ...
Notes
... • Polymers (long chains) of AMINO ACIDS – arranged in specific sequence – linked by PEPTIDE BONDS – range in length from a few to 1000+ ...
... • Polymers (long chains) of AMINO ACIDS – arranged in specific sequence – linked by PEPTIDE BONDS – range in length from a few to 1000+ ...
Lecture 3
... In case of a homomultimer the chains are of one kind whereas for a heteromultimer two or more different chains form the protein. (e.g. Hemoglobin is a heterotetramer. It has two alpha chains and two beta chains.) Proteins may be simple or conjugated – Simple – composed only of amino acid residues Co ...
... In case of a homomultimer the chains are of one kind whereas for a heteromultimer two or more different chains form the protein. (e.g. Hemoglobin is a heterotetramer. It has two alpha chains and two beta chains.) Proteins may be simple or conjugated – Simple – composed only of amino acid residues Co ...
Protein domain
A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three-dimensional structure and often can be independently stable and folded. Many proteins consist of several structural domains. One domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. Domains vary in length from between about 25 amino acids up to 500 amino acids in length. The shortest domains such as zinc fingers are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be ""swapped"" by genetic engineering between one protein and another to make chimeric proteins.