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	The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states
	Ge, Meng ; Pan, Xian-Ming
	2010-10-12 ; 2010-10-12
关键词	Protein stability Cis-trans isomerization Circular dichroism Unfolding ASPERGILLUS-AWAMORI PHAGE-T4 LYSOZYME FREE-ENERGY THERMOSTABILITY STABILIZATION MUTATIONS SSH10B SUBSTITUTIONS DENATURATION DNA Biochemistry & Molecular Biology Microbiology
中文摘要	It has long been understood that the proline residue has lower configurational entropy than any other amino acid residue due to pyrrolidine ring hindrance. The peptide bond between proline and its preceding amino acid (Xaa-Pro) typically exists as a mixture of cis- and trans-isomers in the unfolded protein. Cis-trans isomerization of Xaa-Pro peptide bonds are infrequent, but still occur in folded proteins. Therefore, the effects of the cis-trans isomerization equilibrium in both unfolded and folded states should be taken into account when estimating the stability contribution of a specific proline residue. In order to study the stability contribution of the four proline residues to the hyperthermophilic protein Ssh10b, in this work, we expressed and purified a series of Pro -> Ala mutants of Ssh10b, and performed correlative unfolding experiments in detail. We proposed a new unfolding model including proline isomerization. The model predicts that the contribution of a proline residue to protein stability is associated with the thermodynamic equilibrium between cis- and trans-isomers both in the unfolded and folded states, agreeing well with the experimental results.
语种	英语 ; 英语
出版者	SPRINGER TOKYO ; TOKYO ; 1-11-11 KUDAN-KITA, CHIYODA-KU, TOKYO, 102-0073, JAPAN
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/81856]
专题	清华大学
推荐引用方式 GB/T 7714	Ge, Meng,Pan, Xian-Ming. The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states[J],2010, 2010.
APA	Ge, Meng,&Pan, Xian-Ming.(2010).The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states..
MLA	Ge, Meng,et al."The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states".(2010).

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