Spectroscopic studies of wild-type and mutant "zinc finger" peptides: determinants of domain folding and structure.
about
A CCHC metal-binding domain in Nanos is essential for translational regulation.Metal binding properties of single amino acid deletion mutants of zinc finger peptides: studies using cobalt(II) as a spectroscopic probe.Tri6 encodes an unusual zinc finger protein involved in regulation of trichothecene biosynthesis in Fusarium sporotrichioides.Functional mapping of SPARC: peptides from two distinct Ca+(+)-binding sites modulate cell shapeMutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivationHuman nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).Metal binding and folding properties of a minimalist Cys2His2 zinc finger peptide.Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains.Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate.Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations.Stereochemical basis of DNA recognition by Zn fingers.Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures.The cysteine-rich domain of human proteins, neuronal chimaerin, protein kinase C and diacylglycerol kinase binds zinc. Evidence for the involvement of a zinc-dependent structure in phorbol ester binding.Structures of DNA-binding mutant zinc finger domains: implications for DNA binding.N-Terminal domain of HTLV-I integrase. Complexation and conformational studies of the zinc finger.Zinc is required for folding and binding of a single zinc finger to DNAZinc is required for structural stability of the C-terminus of archaeal translation initiation factor aIF2β
P2860
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P2860
Spectroscopic studies of wild-type and mutant "zinc finger" peptides: determinants of domain folding and structure.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Spectroscopic studies of wild- ...... domain folding and structure.
@en
Spectroscopic studies of wild- ...... domain folding and structure.
@nl
type
label
Spectroscopic studies of wild- ...... domain folding and structure.
@en
Spectroscopic studies of wild- ...... domain folding and structure.
@nl
prefLabel
Spectroscopic studies of wild- ...... domain folding and structure.
@en
Spectroscopic studies of wild- ...... domain folding and structure.
@nl
P2093
P2860
P356
P1476
Spectroscopic studies of wild- ...... domain folding and structure.
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.1.137
P407
P577
1990-01-01T00:00:00Z