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Lectur e 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964 <your question>

Lecture 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964

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Page 1: Lecture 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964

Lecture 5

Web: pollev.com/ucibio

Text: To: 37607Type in: 169964 <your

question>

Page 2: Lecture 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964

OK. What does this all have to do with enzymes?

Anfinsen’s experiment

Took a protein (AP) & forced it to unfold

- Protein lost activityTherefore:______________________________Allowed protein to recover

- Over time, activity returned

Therefore:______________________________

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What does a protein need in order to fold?

Protein folding information contained in

primary amino acid

sequence!OK. But how does amino acid sequence

“fold?”

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Peptide bond is planar…

Page 5: Lecture 5 Web: pollev.com/ucibio Text: To: 37607 Type in: 169964

…but not bonds on either side!

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Rotation of bonds around peptide bond

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Peptide backbone rotation

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“Folding” proteins

Amino acids have different propertiesDifferent preferred Psi and Phi anglesBonds can rotate and pivot

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Secondary structure

3D structure

H-bonds between C=O & N-H

C=O & N-H of peptide bonds

Close together in primary structure

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Folding into secondary structures

Bond rotation causes secondary structurea-helix

b-sheet

Bends, Loops, Disordered

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The a-helix: Annotate

Different parameters define a-helix

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b-Sheet: Annotate

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b-Sheets

Sheets can be twisted

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Bends / Loops

Bends or Loops: ImportantStructured/Unstructured

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Tertiary structrue

Bring secondary structure elements together

Hydrophobic interactions important

Unstructured regions important

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The a-helix

Arrangement of side chains important

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Tertiary structure

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Tertiary structrue

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