Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states.

Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Research Abstract Details 

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Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Abstract Text:

Xiaoye Yang,Min Wang,Michael C Fitzgerald,

Here we investigate the role of backbone-backbone hydrogen bonding interactions in stabilizing the protein folding transition states of two model protein systems, the B1 domain of protein L (ProtL) and the P22 Arc repressor. A backbone modified analogue of ProtL containing an amide-to-ester bond substitution between residues 105 and 106 was prepared by total chemical synthesis, and the thermodynamic and kinetic parameters associated with its folding reaction were evaluated. Ultimately, these parameters were used in a Phi-value analysis to determine if the native backbone-backbone hydrogen bonding interaction perturbed in this analogue (i.e. a hydrogen bond in the first beta-turn of ProtL's beta-beta-alpha-beta-beta fold) was formed in the transition state of ProtL's folding reaction. Also determined were the kinetic parameters associated with the folding reactions of two Arc repressor analogues, each containing an amide-to-ester bond substitution in the backbone of their polypeptide chains. These parameters were used together with previously established thermodynamic parameters for the folding of these analogues in Phi-value analyses to determine if the native backbone-backbone hydrogen bonding interactions perturbed in these analogues (i.e. a hydrogen bond at the end of the intersubunit beta-sheet interface and hydrogen bonds at the beginning of the second alpha-helix in Arc repressor's beta-alpha-alpha structure) were formed in the transition state of Arc repressor's folding reaction. Our results reveal that backbone-backbone hydrogen bonding interactions are formed in the beta-turn and alpha-helical transition state structures of ProtL and Arc repressor, respectively; and they were not formed in the intersubunit beta-sheet interface of Arc repressor, a region of Arc repressor's polypeptide chain previously shown to have other non-native-like conformations in Arc's protein folding transition state.

Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Publishing Authors By Initials

X Yang,M Wang,MC Fitzgerald,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of molecular biology

VOLUME: 363

Page Numbers: 506-19

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 29

MONTH: 07

YEAR: 2006

Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states. Information

Substance Name: Viral Proteins

Registry Number: 0

Grant and Affiliation Information for Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states.

AFFILIATION: Department of Chemistry, Duke University, Durham, NC 27708, USA.

Country: England

AGENCY: United States NIGMS

GRANT: R01-GM61680

ACRONYM: GM

MEDLINETA: J Mol Biol

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