Sandbox Reserved 197: Difference between revisions
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[[Image:proteopedia 2d2.png|thumb|450px|Structure of RNase A. Disulfide bonds between cysteine residues are shown in red and proline residues are shown in green. Pink regions indicate β-sheets, blue regions indicate α-helixes and tan regions indicate loop structures.]] | [[Image:proteopedia 2d2.png|thumb|450px|Structure of RNase A. Disulfide bonds between cysteine residues are shown in red and proline residues are shown in green. Pink regions indicate β-sheets, blue regions indicate α-helixes and tan regions indicate loop structures.]] | ||
== '''Introduction''' == | == '''Introduction''' == | ||
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== '''Protein Folding''' == | == '''Protein Folding''' == | ||
Interatomic interactions are responsible for formation of a protein's 3D structure [http://en.wikipedia.org/wiki/Protein_folding]. Several of these interactions have been identified by the use of site directed mutagenesis to wildtype RNase A and subsequent comparison of the crystal structure to the wildtype. | Interatomic interactions are responsible for formation of a protein's 3D structure [http://en.wikipedia.org/wiki/Protein_folding]. Several of these interactions have been identified by the use of site directed mutagenesis to wildtype RNase A and subsequent comparison of the crystal structure to the wildtype. | ||
<Structure load='7RSA' size='500' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_197/Rnase_a_wild_type/1' /> | |||
==='''Proline Conformation'''=== | ==='''Proline Conformation'''=== | ||
