Defining solution conformations of small linear peptides.
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A novel phosphotyrosine motif with a critical amino acid at position -2 for the SH2 domain-mediated activation of the tyrosine phosphatase SHP-1Solution structure of Compstatin, a potent complement inhibitorStructural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein foldingStructure of neurolysin reveals a deep channel that limits substrate accessLength-dependent stability and strand length limits in antiparallel -sheet secondary structureStructure of human parathyroid hormone 1-37 in solutionCrystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationA short linear peptide that folds into a native stable beta-hairpin in aqueous solutionConformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREBConstraining cyclic peptides to mimic protein structure motifs.Identification and structure characterization of a Cdk inhibitory peptide derived from neuronal-specific Cdk5 activator.Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data.Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptideStructural determinants present in the C-terminal binding protein binding site of adenovirus early region 1A proteins.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. I. Importance of hydrophobic interactions in stabilization of beta-hairpin structure.Solution state structures of human pancreatic amylin and pramlintide.Nuclear magnetic resonance analysis of solution conformations in C4-V3 hybrid peptides derived from human immunodeficiency virus (HIV) type 1 gp120: relation to specificity of peptide-induced anti-HIV neutralizing antibodiesOptimization of rates of protein folding: the nucleation-condensation mechanism and its implications.Influence of solvent and intramolecular hydrogen bonding on the conformational properties of o-linked glycopeptidesbeta-hairpin-forming peptides; models of early stages of protein folding.Probing alpha-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation.Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 AgonistPeptide interactions with G-protein coupled receptors.NMR investigations of structural and dynamics features of natively unstructured drug peptide - salmon calcitonin: implication to rational design of potent sCT analogs.Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Structure and orientation of pardaxin determined by NMR experiments in model membranes.Proline-glutamate chimera's side chain conformation directs the type of β-hairpin structure.A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.Peptide mimotopes of malondialdehyde epitopes for clinical applications in cardiovascular disease.Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same foldFolding propensities of peptide fragments of myoglobin.The turn sequence directs beta-strand alignment in designed beta-hairpins.Helix formation and the unfolded state of a 52-residue helical protein.Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: implications for the structure of continuous peptide epitopes of proteins.A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin.T1BT* structural study of an anti-plasmodial peptide through NMR and molecular dynamicsRole of hydrophobic interactions and desolvation in determining the structural properties of a model alpha beta peptide.
P2860
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P2860
Defining solution conformations of small linear peptides.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Defining solution conformations of small linear peptides.
@en
Defining solution conformations of small linear peptides.
@nl
type
label
Defining solution conformations of small linear peptides.
@en
Defining solution conformations of small linear peptides.
@nl
prefLabel
Defining solution conformations of small linear peptides.
@en
Defining solution conformations of small linear peptides.
@nl
P1476
Defining solution conformations of small linear peptides.
@en
P2093
P304
P356
10.1146/ANNUREV.BB.20.060191.002511
P577
1991-01-01T00:00:00Z