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The effect of additional disulfide bonds on the stability and folding of ribonuclease A

✍ Scribed by Pascal Pecher; Ulrich Arnold

Book ID
108074466
Publisher
Elsevier Science
Year
2009
Tongue
English
Weight
598 KB
Volume
141
Category
Article
ISSN
0301-4622

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πŸ“œ SIMILAR VOLUMES

Further experimental studies of the disu
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Two very different mechanisms of folding have been proposed from experimental studies of disulfide formation in reduced ribonuclease A. (1) A pathway in which the rate-limiting step separates fully folded protein from all other disulfide intermediates and occurs solely in three-disulfide intermediat

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## Abstract An understanding of the forces that contribute to stability is pivotal in solving the protein‐folding problem. Classical theory suggests that disulfide bonds stabilize proteins by reducing the entropy of the denatured state. More recent theories have attempted to expand this idea, sugge

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The kinetics of folding of the two forms of unfolded ribonuclease A have been measured as a function of solvent viscosity by adding either glycerol or sucrose. The aim is to find out if either reaction is rate limited by segmental motion whose rate depends on external friction. The fast folding rea