User:Michael Roberts/BIOL115 Myo: Difference between revisions
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You see how the <scene name='User:Michael_Roberts/BIOL115_Myo/Hbonds/1'>hydrogen bonds</scene> (yellow) that maintain the main secondary structure of the protein are arranged in this next view. | You see how the <scene name='User:Michael_Roberts/BIOL115_Myo/Hbonds/1'>hydrogen bonds</scene> (yellow) that maintain the main secondary structure of the protein are arranged in this next view. | ||
Some amino acids have specific effects on secondary structure. This next view shows the locations of the <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/11'>PROLINE</scene> residues in myoglobin. You can see that they all fall at the end of a stretch of helix. This is bacause their large side chains do not fit within the straight run of α-helix. | Some amino acids have specific effects on secondary structure. This next view shows the locations of the <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/11'>PROLINE</scene> residues in myoglobin. You can see that they all fall at the end of a stretch of helix. This is bacause their large side chains do not fit within the straight run of α-helix. | ||
'''THE GLOBIN FOLD''': In this next view, the eight <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/3'>individual alpha-helices </scene>are each coloured differently. This gives you an impression of the classic globion fold. The α-helices pack together tightly, and there is very little space in the centre of the protein. | '''THE GLOBIN FOLD''': In this next view, the eight <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/3'>individual alpha-helices </scene>are each coloured differently. This gives you an impression of the classic globion fold. The α-helices pack together tightly, and there is very little space in the centre of the protein. | ||