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An Introduction to Research in Protein Folding for Undergraduates
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Abstract
The objective of this article is to introduce students to current research activity on protein folding via experimentation and a literature survey. Major effort in the field of biophysical chemistry today is focused on elucidating those factors controlling the transformation of a protein from a nascent polypeptide chain to a unique, functionally active three-dimensional structure. The possible involvement of misfolded or aggregated proteins in diseases such as Altzheimer's, cystic fibrosis, and cataracts as well as various neurodegenerative diseases has increased the incentive to solve the "protein folding problem". In this experiment the guanidine-hydrochloride induced protein unfolding of horse heart metmyoglobin is monitored spectrophotometrically via the protein fluorescence emission. The data are analyzed using a simple thermodynamic model which assumes a two-state system and fitted using nonlinear curve fitting. Background information on protein structure, protein fluorescence, simple models for folding, and the use of chaotropic agents is also presented. The experiment is suitable for students in advanced undergraduate chemistry courses such as physical or biophysical chemistry.
Keywords (Audience):
Upper-Division UndergraduateKeywords (Domain):
BiochemistryKeywords (Feature):
Concepts in BiochemistryKeywords (Pedagogy):
Hands-On Learning / ManipulativesKeywords (Subject):
Proteins / PeptidesCiting Articles
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This article has been cited by 11 ACS Journal articles (5 most recent appear below).
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- Received: August 03, 2009
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