Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes.

Journal of the American Chemical Society - 25 Jul 2012

Chung Jean K, Thielges Megan C, Fayer Michael D

Abstract excerpt

Two-dimensional infrared (2D IR) vibrational echo spectroscopy was used to measure the fast dynamics of two variants of chicken villin headpiece 35 (HP35). The CN of cyanophenylalanine residues inserted in the hydrophobic core were used as a vibrational probe. Experiments were performed on both singly (HP35-P) and doubly CN-labeled peptide (HP35-P(2)) within the wild-type sequence, as well as on HP-35 containing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Chickens
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neurofilament Proteins

Share to Nitriles

Share to Peptide Fragments

Share to Protein Conformation

Share to Spectrophotometry, Infrared

Source

Open in PubMed Open full text

Identifiers

PMID: 22764745
DOI: 10.1021/ja303017d
PMCID: PMC3487692

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes.PMID 22764745Read ↗

Mutation of charged residues to neutral ones accelerates urea denaturation of HP-35.Semantic proximity Read ↗

Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements.Semantic proximity Read ↗

High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.Semantic proximity Read ↗

The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier.Semantic proximity Read ↗

High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.Semantic proximity Read ↗

Effect of a serine-to-aspartate replacement on the recognition of chitin oligosaccharides by truncated hevein. A 3D view by using NMR.Semantic proximity Read ↗

Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.Semantic proximity Read ↗

Crystal structure of a pH-stabilized mutant of villin headpiece.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.