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Conformational stability and folding mechanisms of dimeric proteins

✍ Scribed by Jessica A.O. Rumfeldt; Céline Galvagnion; Kenrick A. Vassall; Elizabeth M. Meiering

Book ID
113843488
Publisher
Elsevier Science
Year
2008
Tongue
English
Weight
995 KB
Volume
98
Category
Article
ISSN
0079-6107

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📜 SIMILAR VOLUMES

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Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
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## Abstract The conformational stability of dimeric globular proteins can be measured by equilibrium denaturation studies in solvents such as guanidine hydrochloride or urea. Many dimeric proteins denature with a 2‐state equilibrium transition, whereas others have stable intermediates in the proces

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On the Conformational Stability of Folded Proteins
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The folded native state of a globular protein is noted to be marginally stabilized over the structureless unfolded state by various atomic/group interactions. Quantitative enumeration of these factors remains to be a difficult task to workers in the field. In this work we collect experimental inform