Clustering of large hydrophobes in the hydrophobic core of two-stranded alpha-helical coiled-coils controls protein folding and stability

scientific article published on 03 July 2003

Clustering of large hydrophobes in the hydrophobic core of two-stranded alpha-helical coiled-coils controls protein folding and stability is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M305306200
P698PubMed publication ID12842878

P2093author name stringRobert S Hodges
Stanley C Kwok
P2860cites workPolymer principles and protein foldingQ24672635
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coilQ27655682
Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contractionQ28249121
The role of the dynein stalk in cytoplasmic and flagellar motilityQ28284498
A spring-loaded mechanism for the conformational change of influenza hemagglutininQ28646856
Coiled coils: new structures and new functionsQ29555849
Determination and analysis of urea and guanidine hydrochloride denaturation curvesQ29616644
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfoldingQ29620340
Structure based prediction of protein folding intermediatesQ30420701
Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniquesQ30447247
Local heterogeneity in the pressure denaturation of the coiled-coil tropomyosin because of subdomain folding units.Q31915094
Importance of secondary structural specificity determinants in protein folding: insertion of a native beta-sheet sequence into an alpha-helical coiled-coilQ36639404
A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acidsQ36785218
Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structureQ37504108
Monoclonal anti-DNA antibodies: structure, specificity, and biologyQ41302752
Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives.Q41627541
Analysis of synthetic peptides by high-performance liquid chromatographyQ41629559
Persistence of native-like topology in a denatured protein in 8 M ureaQ43682045
Evaluation of the energetic contribution of interhelical Coulombic interactions for coiled coil helix orientation specificityQ43860216
Long-range interactions within a nonnative proteinQ43901723
Energetics of complementary side-chain packing in a protein hydrophobic coreQ43985354
Regulation of coiled-coil assembly in tropomyosinsQ44028115
The role of unstructured highly charged regions on the stability and specificity of dimerization of two-stranded alpha-helical coiled-coils: analysis of the neck-hinge region of the kinesin-like motor protein Kif3A.Q44028119
Helix capping interactions stabilize the N-terminus of the kinesin neck coiled-coilQ44028122
The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosinQ45337647
Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d".Q52076920
Scanning microcalorimetry in studying temperature-induced changes in proteins.Q52651402
De novo design of native proteins: characterization of proteins intended to fold into antiparallel, rop-like, four-helix bundles.Q54569382
Preferential Heterodimeric Parallel Coiled-coil Formation by Synthetic Max and c-Myc Leucine Zippers: A Description of Putative Electrostatic Interactions Responsible for the Specificity of HeterodimerizationQ58234192
An extended microtubule-binding structure within the dynein motor domainQ59096941
The two-stranded alpha-helical coiled-coil is an ideal model for studying protein stability and subunit interactionsQ68192949
Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effectsQ68460606
Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residuesQ70501773
Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c foldingQ71028920
The heat capacity of proteinsQ71537055
Salt effects on protein stability: two-stranded alpha-helical coiled-coils containing inter- or intrahelical ion pairsQ73306463
The role of helix formation in the folding of a fully alpha-helical coiled coilQ73365490
Thermodynamic analysis of cavity creating mutations in an engineered leucine zipper and energetics of glycerol-induced coiled coil stabilizationQ73660243
Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1Q74300092
Make room for dyneinQ77712643
De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coilsQ77760417
P433issue37
P407language of work or nameEnglishQ1860
P304page(s)35248-35254
P577publication date2003-07-03
P1433published inJournal of Biological ChemistryQ867727
P1476titleClustering of large hydrophobes in the hydrophobic core of two-stranded alpha-helical coiled-coils controls protein folding and stability
P478volume278