trans peptide bond 180 °. 2e structure regular pattern of h-bonding involves backbone (not side...

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Trans peptide bond 180 °

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Page 1: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Trans peptide bond 180 °

Page 2: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 3: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 4: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 5: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 6: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

2e Structure

• Regular pattern of H-bonding• Involves backbone (not side chains)

• C=O …H-N

• Several consecutive residues form 2e structure• a helices b sheets b turns

Page 7: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

5.4 Å/turn

Page 8: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

3.6 residues per turn

H bonding in alpha helix

Page 9: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 10: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 11: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 12: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Parallel and anti parallel strands

Page 13: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 14: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 15: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

B turn

Page 16: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Indicate

Alpha helix

Beta sheet

Whattype ofsidechainsinteract with DNA backbone?

Page 17: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Where are the hydrophic amino acids?Hydrophilic amino acids?

Page 18: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 19: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

2. Suppose a protein has four helices identical to the alpha helix found in Problem 1 and folds into a “four helix bundle” where the alpha helices are packed together. What part of the helices interact with each other? What force stabilizes this bundle? Draw a the four helix bundle from the top and side

Page 20: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Learning Goal—Importance of hydrophobic and hydrophilic amino acids in protein folding.

Page 21: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Can Protein Structure and Function be Predicted from Sequence?

• Globular Proteins• Fibrous Proteins (Hair, hooves, silk, collagen)– Structural– Repeated sequences– Physical properties (strength, flexibility) can be fine-tuned

Page 22: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 23: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Parallel and anti parallel strandsSilk=fibroinExtended b sheets

Page 24: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

a-helical coiled-coila-keratin (wool, hair, skin)Myosin & tropomyosin (muscles)

Long fibersHeptad repeat

Page 25: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Heptad repeatCoiled-coil

Page 26: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Collagen Triple helix

Page 27: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Collagen Triple Helix

Page 28: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Held together by H-bonds between strands

Hydroxy Proline also H-bonds

3000 nm long x 1.5 nm diameter 800 aa’s per strand300,000 g/mol for triple strand

Page 29: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues
Page 30: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Vitamin C requiredTo make HYP

Scurvy= Vitamin CDeficiencyfragilecollagen

Triple strands also heldTogether by covalent links=CrosslinkingIntra- and inter strandHIS-hydroxylysineAging more xlinksstiffer,less flexible

Page 31: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Medical Application

• Cornea of eye contains collagen• Keratoconus– Excessive astigmatism– Progressively worse vision not correctable– Cornea bulges becomes very bent and thin

• Treatment– Corneal transplant– Special contact lenses– Laser crosslinking as early as possible

Page 32: Trans peptide bond 180 °. 2e Structure Regular pattern of H-bonding Involves backbone (not side chains) C=O … H-N Several consecutive residues

Experimental Methods--Spectroscopy

• Circular Dichroism– Depends on chirality– Native or denatured– % of each 2e structure

• Infrared • NMR Ca chemical shift