Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin.
about
Probing the roles of two tryptophans surrounding the unique zinc coordination site in lipase family I.5Thermal unfolding of smooth muscle and nonmuscle tropomyosin alpha-homodimers with alternatively spliced exonsProtein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.Tropomyosin 1: Multiple roles in the developing heart and in the formation of congenital heart defectsStructure-function analysis of the HrpB2-HrcU interaction in the Xanthomonas citri type III secretion system.Tropomyosin-based regulation of the actin cytoskeleton in time and space.Defining the minimum size of a hydrophobic cluster in two-stranded alpha-helical coiled-coils: effects on protein stability.Instability in the central region of tropomyosin modulates the function of its overlapping ends.Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization.Non-natural amino acid fluorophores for one- and two-step fluorescence resonance energy transfer applications.Identification of a unique "stability control region" that controls protein stability of tropomyosin: A two-stranded alpha-helical coiled-coil.Different effects of trifluoroethanol and glycerol on the stability of tropomyosin helices and the head-to-tail complex.Ca2+-induced rolling of tropomyosin in muscle thin filaments: the alpha- and beta-band hypothesis revisited.Charged residue changes in the carboxy-terminus of alpha-tropomyosin alter mouse cardiac muscle contractility.Charged residue alterations in the inner-core domain and carboxy-terminus of alpha-tropomyosin differentially affect mouse cardiac muscle contractility.Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils.
P2860
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P2860
Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin.
description
2002 nî lūn-bûn
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name
Specific sequences determine t ...... -terminal half of tropomyosin.
@en
Specific sequences determine t ...... -terminal half of tropomyosin.
@nl
type
label
Specific sequences determine t ...... -terminal half of tropomyosin.
@en
Specific sequences determine t ...... -terminal half of tropomyosin.
@nl
prefLabel
Specific sequences determine t ...... -terminal half of tropomyosin.
@en
Specific sequences determine t ...... -terminal half of tropomyosin.
@nl
P2093
P2860
P356
P1476
Specific sequences determine t ...... -terminal half of tropomyosin.
@en
P2093
Adriana A Paulucci
Alessandra Machado
Chuck S Farah
Cyril M Kay
Leslie Hicks
M Teresa M Miranda
P2860
P304
39574-39584
P356
10.1074/JBC.M204749200
P407
P577
2002-08-07T00:00:00Z