Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

Item
http://www.wikidata.org/entity/Q36281564
An engineered leucine zipper a position mutant with an unusual three-state unfolding pathwayAlternative splice variants in TIM barrel proteins from human genome correlate with the structural and evolutionary modularity of this versatile protein foldMapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.Random dissection to select for protein split sites and its application in protein fragment complementationBetaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins.Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscapeAnatomy of protein structures: visualizing how a one-dimensional protein chain folds into a three-dimensional shape.NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Random-coil behavior and the dimensions of chemically unfolded proteins.Rat liver betaine-homocysteine S-methyltransferase equilibrium unfolding: insights into intermediate structure through tryptophan substitutions.Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraints.Folding and unfolding of gammaTIM monomers and dimers.In vivo fragment complementation of a (beta/alpha)(8) barrel protein: generation of variability by recombination.The stability of the TIM-barrel domain of a psychrophilic chitinase.Search for independent (β/α)4 subdomains in a (β/α)8 barrel β-glucosidase.Roles for the two N-terminal (β/α) modules in the folding of a (β/α)₈-barrel protein as studied by fragmentation analysis.
P2860

Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

Item
http://www.wikidata.org/entity/Q36281564
description
1999 nî lūn-bûn
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1999年の論文
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1999年学术文章
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1999年学术文章
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1999年学术文章
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1999年学术文章
@zh-my
1999年学术文章
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1999年學術文章
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1999年學術文章
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1999年學術文章
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name
Identifying the structural bou ...... , a beta/alpha barrel protein.
@ast
Identifying the structural bou ...... , a beta/alpha barrel protein.
@en
type
label
Identifying the structural bou ...... , a beta/alpha barrel protein.
@ast
Identifying the structural bou ...... , a beta/alpha barrel protein.
@en
prefLabel
Identifying the structural bou ...... , a beta/alpha barrel protein.
@ast
Identifying the structural bou ...... , a beta/alpha barrel protein.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P921
P932
P356
P1433
P1476
Identifying the structural bou ...... , a beta/alpha barrel protein.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P921
P932