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 Fast Atom Bombardment Mass Spectrometry [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. FABMS is ~~done~~ by mixing the material to be analyzed (RNase A) with a non-volatile environment called a matrix and then bombarded by high energy molecules within a vacuum. Through this technique it has been found that RNase A is composed of four anti-parallel β-sheets and three α-helixes. Presence of four disulfide bonds and two ''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 Fast Atom Bombardment Mass Spectrometry [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. FABMS is performed by mixing the material to be analyzed (RNase A) with a non-volatile environment called a matrix and is then bombarded by high energy molecules within a vacuum. Through this technique it has been found that RNase A is composed of four anti-parallel β-sheets and three α-helixes. Presence of four disulfide bonds and two ''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 for his work on protein folding, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure. The Anfinsen experiment has ignited the interest in protein folding. Today, the correlation between the amino acid sequence and the tertiary structure of RNase A continues to serve as a model for protein folding.

== '''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 Fast Atom Bombardment Mass Spectrometry [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  FABMS is done by mixing the material to be analyzed (RNase A) with a non-volatile environment called a matrix and then bombarded by high energy molecules within a vacuum.  Through this technique it has been found that RNase A is composed of four anti-parallel β-sheets and three α-helixes. Presence of four disulfide bonds and two ''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 Fast Atom Bombardment Mass Spectrometry [http://en.wikipedia.org/wiki/Fast_atom_bombardment].  FABMS is performed by mixing the material to be analyzed (RNase A) with a non-volatile environment called a matrix and is then bombarded by high energy molecules within a vacuum.  Through this technique it has been found that RNase A is composed of four anti-parallel β-sheets and three α-helixes. Presence of four disulfide bonds and two ''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 for his work on protein folding, RNase A has been shown to spontaneously fold back into its native conformation following degradation to its primary structure.  The Anfinsen experiment has ignited the interest in protein folding. Today, the correlation between the amino acid sequence and the tertiary structure of RNase A continues to serve as a model for protein folding.
 == '''Protein Folding''' ==