Fichas
tertiary structure
Fichas del conjunto (8)
- 1Folding of polypeptide chainR groups interact
- 2Hphobic interactions- Hphobic clusters of non-polar AA
- disrupted by heat or organic solvents or denaturing agents - 3H bonds- involve uncharged polar R groups
- disrupted by heat, denaturing agents or water - 4electrostatic bonds- ionic interactions, salt bridges
- needs charged residues (determined by pH)
- disrupted by changes in pH
- need to be surrounded by Hphobic interactions to work - 5van der waal bonds- weak electrostatic forces
- work over a short rang effect
- broken by heat or denaturing agents - 6phosphorylation- can change the charge of an R group by a molecular switch
- 7Disulphide bonds- important
- locks the protein into a certain shape in the endoplasmic recticulum
- can use covalent bonds - 8anfinsen's exp on ribonuclease- the folded active form of a protein has the lowest free energy
- all info on how the protein will fold is told in primary structure
- not all proteins fold easily, they may need protein disulphide isomerase - this makes and breaks disulphide bonds until the correct conformation is made
- exp doesn't work on all proteins
Información
- Descripción
- (2) Protein types, structures n bonds) Macromolecules of Life Fichas sobre tertiary structure, creado por Fatima Farhan el 03/01/2019.
- Creado por
- Fatima Farhan
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