Design of a hyperstable protein by rational consideration of unfolded state interactions.

Design of a hyperstable protein by rational consideration of unfolded state interactions. Research Abstract Details 

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Design of a hyperstable protein by rational consideration of unfolded state interactions. Abstract Text:

Burcu Anil,Rebecca Craig-Schapiro,Daniel P Raleigh,

Stabilization of proteins is a long-sought objective. Targeting the unfolded state interactions of a protein is not a method used for this purpose, although many proteins are known to contain such interactions. The N-terminal domain of ribosomal protein L9 (NTL9) has a lysine residue at position 12, which makes strong non-native interactions in the unfolded state. Substitution of a d-alanine for G34 in NTL9 is known to stabilize the protein by reducing the entropy of the unfolded state. Here we combine these two mutations to design a hyperstable protein. The structure of the variant is the same as that of wild-type as judged by 2D NMR. The variant is hyperstable as judged by denaturation experiments, where complete thermal unfolding of the protein does not occur in native buffer.

Design of a hyperstable protein by rational consideration of unfolded state interactions. Publishing Authors By Initials

B Anil,R Craig-Schapiro,DP Raleigh,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Design of a hyperstable protein by rational consideration of unfolded state interactions. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of the American Chemical Society

VOLUME: 128

Page Numbers: 3144-5

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 15

MONTH: Mar

YEAR: 2006

Design of a hyperstable protein by rational consideration of unfolded state interactions. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Design of a hyperstable protein by rational consideration of unfolded state interactions. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: chemistry

Chemical & Substance for Abstract: Design of a hyperstable protein by rational consideration of unfolded state interactions. Information

Substance Name: Alanine

Registry Number: 56-41-7

Grant and Affiliation Information for Design of a hyperstable protein by rational consideration of unfolded state interactions.

AFFILIATION: Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM70941

ACRONYM: GM

MEDLINETA: J Am Chem Soc

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