Conformation: Difference between revisions
CSV import |
No edit summary |
||
| Line 34: | Line 34: | ||
{{stub}} | {{stub}} | ||
{{No image}} | {{No image}} | ||
Latest revision as of 16:51, 22 March 2025
Conformation refers to the spatial arrangement of atoms in a molecule and the changes it undergoes. In the field of biochemistry, conformation often refers to the shape of a protein or other macromolecule, based on the spatial location of its atoms.
Overview[edit]
In the context of biochemistry, conformation is the shape adopted by a molecule as a result of rotational movement of groups about single bonds. This is particularly relevant in large molecules like proteins and nucleic acids, where simple rotation around a single bond can lead to a completely different molecular shape, and thus different function.
Conformation in Proteins[edit]
Proteins are made up of amino acids linked together by peptide bonds. The sequence of amino acids in a protein, its primary structure, determines its shape and function. However, the protein can adopt different conformations depending on the conditions, such as pH or temperature.
Conformation in Nucleic Acids[edit]
Nucleic acids, such as DNA and RNA, can also adopt different conformations. The most common conformation for DNA is the B-form, which is a right-handed helix. However, DNA can also adopt A-form and Z-form conformations under certain conditions.
Factors Influencing Conformation[edit]
Several factors can influence the conformation of a molecule. These include:
- Steric hindrance: Large groups can hinder the rotation around a bond, forcing the molecule into a certain conformation.
- Electrostatic interactions: The presence of charged groups can influence the conformation of a molecule.
- Hydrogen bonding: Hydrogen bonds can stabilize certain conformations.
- Van der Waals forces: These weak interactions can also influence the conformation of a molecule.


