This is the secondary folding phase where hydrogen bonds between the side chains give you the alpha helix and the beta pleated sheet.
Rough endoplasmic reticulum.Rough endoplasmic reticulumB.Rough endoplasmic reticulum
NUCLEUS FUNCTION-Protein translocation, folding and transport or protein.
it is endergonic because it reduces entropy
Proteins are composed of amino acids, each of which have their own special properties. The non-polar amino acids would fold into the interior of the protein during protein folding, because they are hydrophobic. A protein consists of a primary structure, which consists of the amino acid chain. The secondary structure is how the amino acids join together into alpha helices and beta pleated chains and form hydrogen bonds. The tertiary structure is when disulphide bridges form, which maintain the protein's 3D shape, and the 3D shape begins to emerge. The quaternary structure is an assortment of several polypeptides, and constitutes the entire protein. The final shape of the protein determines its function.For example an enzyme carry out catalytic functions are mainly accomplished by it's catalytic core residues(place where substrate binds). when the 3D structure of protein is properly made(folded) then it is active, when a single residue is mutated or any improper folding leads to the enzyme either hyperactive, poorly active or inactive.
Proteins have a number of 'levels' of structure associated with them: Primary, Secondary, Tertiatry and Quaternary.Primary StructureThe order of amino acids in a protein determines it's primary structure.Secondary StructureThe secondary structure is the simple folding of a protein into a shape. The two general shapes found are the alpha-helix (like a spiral) and the beta-pleated sheet (a little like the zigzag shape of a concertina). These shapes result from the intermolecular forces between R-groups on amino acids, and in the case of cystine, disulphide bridges.Tertiary StructureThe tertiary structure is a further layer of folding of the secondary structure. Single-chain proteins reach their final form with this layer of folding.Quaternery StructureOnly found in multi-unit protein complexes such as haemoglobin. This is a level involving the binding together of multiple protein chains to form a final structure. In the case of haemoglobin, this involves 4 main protein chains surrounding an Fe2+ ion.
The alpha helix and beta sheets are found at the Secondary level of protein folding. It's when the protein is taking its shape. Secondary structure
The tertiary structure is the folding
secondary structure of a protein
Translation and transcription. Then they go into protein folding.
secondary structure
together they make a secondary protein structure
Rough endoplasmic reticulum.Rough endoplasmic reticulumB.Rough endoplasmic reticulum
The secondary genetic code is the folding of protein.
The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.
Proteins have primary structure, which is their amino acid sequence, secondary structure, which is either the alpha helix or the beta pleated sheet, tertiary structure, the protein's geometric shape, and quaternary structure, the arrangement of multiple protein subunits.
Chaperonins
A chaperone protein is used in the cell to ensure proper protein folding, among other cellular functions.