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Creado por J yadonknow
hace más de 6 años
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Pregunta | Respuesta |
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 |
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