Prab: CSV import

2025-02-18T11:03:41Z

CSV import

← Older revision		Revision as of 11:03, 18 February 2025
Line 32:		Line 32:
	{{Biochemistry-stub}}		{{Biochemistry-stub}}
	{{Molecular-biology-stub}}		{{Molecular-biology-stub}}
			== Protein_structure ==
			<gallery>
			File:Protein_structure.png\|Protein structure
			File:Alpha_helix.png\|Alpha helix
			File:Domain_Homology.png\|Domain homology
			File:Schematic_view_of_the_two_main_ensemble_modeling_approaches.jpg\|Schematic view of the two main ensemble modeling approaches
			File:Protein_structure_examples.png\|Protein structure examples
			File:Rate_of_Protein_Structure_Determination-2014.png\|Rate of protein structure determination (2014)
			</gallery>

Prab: CSV import

2024-03-22T12:14:15Z

CSV import

New page

'''Protein structure''' refers to the three-dimensional arrangement of atoms in an [[amino acid]]-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of [[amino acids]], the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Protein structure has a four-level hierarchy: the primary, secondary, tertiary, and quaternary structures.

==Primary structure==
The '''primary structure''' of a protein refers to the sequence of amino acids in the polypeptide chain. The primary structure is held together by peptide bonds, which are made during the process of [[protein biosynthesis]]. The sequence of amino acids determines the protein's shape and function. Alterations in the primary structure can significantly affect a protein's properties.

==Secondary structure==
The '''secondary structure''' is the form of local folded structures that form within a polypeptide due to interactions between atoms of the backbone. The most common secondary structures are [[alpha helix|alpha helices]] and [[beta sheet|beta sheets]]. Hydrogen bonds between the backbone atoms form these structures. Secondary structures are often regionally distinct within the protein and contribute to the overall fold of the protein.

==Tertiary structure==
The '''tertiary structure''' describes the three-dimensional structure of a single protein molecule. The tertiary structure is what determines the protein's function. It is stabilized by various interactions, including hydrogen bonds, ionic bonds, Van der Waals forces, and hydrophobic packing. The tertiary structure can be significantly altered by changes in [[pH]], temperature, and the presence of other molecules, which can lead to protein denaturation.

==Quaternary structure==
The '''quaternary structure''' refers to the structure formed by several protein molecules (polypeptides), often called protein subunits, which function as a single protein complex. Quaternary structures are stabilized by the same non-covalent interactions that stabilize tertiary structures. Proteins with quaternary structures include hemoglobin, DNA polymerase, and ion channels.

==Protein folding==
Protein folding is the process by which a protein structure assumes its functional shape or conformation. It is a crucial step in the translation of genetic information into functional molecules. Misfolded proteins can lead to diseases such as Alzheimer's, Parkinson's, and prion diseases.

==Protein structure prediction==
Protein structure prediction is a field of bioinformatics that deals with the prediction of the three-dimensional structure of proteins based on their amino acid sequences. This is important for understanding the function of proteins and for designing new drugs.

==See also==
* [[Protein biosynthesis]]
* [[Protein domain]]
* [[Protein function prediction]]
* [[Protein-protein interaction]]
* [[Structural biology]]

[[Category:Protein structure]]
[[Category:Biochemistry]]
[[Category:Molecular biology]]

{{Biochemistry-stub}}
{{Molecular-biology-stub}}

Protein structure - Revision history

Prab: CSV import

Prab: CSV import