Protein III

Question	Answer
What are salt bridges?	Ion pair bond
What is a domain?	Globular unit formed from part of a polypeptide often associated with a particular function
What does a large domain bind?	ATP, glucose binds between (?)
What feature does a domain have?	Flexibility between them so enzymes can clamp down on substrate
What is a scissile bond?	Covalent bond prone to cleavage by enzyme activity
What is HIV Protease structure and function?	Cleaves polyproteins into protein subunits, has Asp-Thr-Gly, common to aspartic proteases Aspartate - hydrophilic, Nucleophile water works with aspartic acid to cleave scissile peptide bond
How does hydrogen bonding differ in B to A?	Beta- H bonds form between residues of different polypeptide chains between the C=O O atom and the N of the NH2 group In alpha, H bonding occurs within the chain
Which is generally more stable? Antiparallel or parallel bonding?	Antiparallel, H bonds are better aligned in this configuration
What are disulphide bridges?	Bonding unique to cysteine residues, thiol groups form disulphide bridges via oxidative folding
What is the implication of sulphide bonding?	Enforces angle restraints on C-beta and S-gamma atoms of adjacent cysteines, in RNase A destabilises unfolded state by reducing its entropy, makes globular 3D shape more energetically favourable Promote 3D folding into tertiary state and maintains secondary state

Resource summary

	Created by J yadonknow over 6 years ago