Sandbox Reserved 197: Difference between revisions

Line 5:

== '''Introduction''' ==

Ribonuclease A is an enzyme found in the pancreas that is involved in catalyzing RNA degradation. The kidney-shaped structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. RNase A is composed of four anti-parallel β-sheets and three α-helixes. The <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Presence of four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/anfinsen-bio.html]. Perhaps most widely known as the protein that helped Christian Anfinsen win the Nobel Prize, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure. This experiment has ignited the interest in protein folding and its characterisitcs that is observed today and the idea behind protein folding that "sequence determines structure."

Ribonuclease A is an enzyme found in the pancreas that is involved in catalyzing RNA degradation. The kidney-shaped structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. RNase A is composed of four anti-parallel β-sheets and three α-helixes. The <scene name='Sandbox_Reserved_197/Active_site/2'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Presence of four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/anfinsen-bio.html]. Perhaps most widely known as the protein that helped Christian Anfinsen win the Nobel Prize, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure. This experiment has ignited the interest in protein folding and its characterisitcs that is observed today and the idea behind protein folding that "sequence determines structure."

== '''Protein Folding''' ==

Sandbox Reserved 197: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 5: / Line 5: @@
 == '''Introduction''' ==
-Ribonuclease A is an enzyme found in the pancreas that is involved in catalyzing RNA degradation.  The kidney-shaped structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  RNase A is composed of four anti-parallel β-sheets and three α-helixes. The <scene name='Sandbox_Reserved_197/Active_site/1'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Presence of four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/anfinsen-bio.html].  Perhaps most widely known as the protein that helped Christian Anfinsen win the Nobel Prize, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure.  This experiment has ignited the interest in protein folding and its characterisitcs that is observed today and the idea behind protein folding that "sequence determines structure."
+Ribonuclease A is an enzyme found in the pancreas that is involved in catalyzing RNA degradation.  The kidney-shaped structure of RNase A has been determined through crystallography [http://en.wikipedia.org/wiki/Crystallography] and FABMS [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  RNase A is composed of four anti-parallel β-sheets and three α-helixes. The <scene name='Sandbox_Reserved_197/Active_site/2'>active site</scene> lies within the cleft and houses three residues important for catalysis: His12, His119, and Lys41. Presence of four disulfide bonds and four ''cis'' proline residues greatly effect the structure and folding kinetics of RNase A [http://nobelprize.org/nobel_prizes/chemistry/laureates/1972/anfinsen-bio.html].  Perhaps most widely known as the protein that helped Christian Anfinsen win the Nobel Prize, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure.  This experiment has ignited the interest in protein folding and its characterisitcs that is observed today and the idea behind protein folding that "sequence determines structure."
 == '''Protein Folding''' ==