User:Michael Roberts/BIOL115 Myo: Difference between revisions

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'''THE GLOBIN FOLD''':
'''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 helices pack together tightly, and there is very little space in the centre of the protein.
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 helices pack together tightly, and there is very little space in the centre of the protein.
'''HYDROPHOBICITY''':
Globular folds like this are characterised by a polar, <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/4'>hydrophilic exterior</scene>, which interacts with the aqueous solvent, and a hydrophobic core.
This view shows a section through the protein that highlights the <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/5'>hydrophobic core </scene>better.
This view has been produced in the software by a process known as 'slabbing'. You can still rotate the molecule around - whatever view you see will the the front part of the view of the protein cut off.


</StructureSection>
</StructureSection>