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

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.

Journal of the American Chemical Society - 9 Sept 2009

Hansen D Flemming, Vallurupalli Pramodh, Kay Lewis E

Abstract excerpt

An understanding of many biological processes can only be achieved through studies of the structure (enthalpy) and motions (entropy) of the key molecules that are involved, including those that are formed only transiently and with low population. These transiently formed, low populated states are invisible to most biophysical techniques but in many cases they can be studied in detail using relaxation dispersion...

Read the complete abstract on PubMed

Topics

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

Share to Magnetic Resonance Spectroscopy
Share to Movement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Denaturation

Share to Protein Folding

Share to Proteins

Share to Proto-Oncogene Proteins c-fyn

Share to Reproducibility of Results

Share to src Homology Domains

Source

Identifiers

PMID: 19685870
DOI: 10.1021/ja903897e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Measurement of methyl group motional parameters of invisible, excited protein states by NMR spectroscopy.PMID 19685870Read ↗

Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Semantic proximity Read ↗

Studying "invisible" excited protein states in slow exchange with a major state conformation.Semantic proximity Read ↗

Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain.Semantic proximity Read ↗

Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.Semantic proximity Read ↗

Separating degenerate (1)H transitions in methyl group probes for single-quantum (1)H-CPMG relaxation dispersion NMR spectroscopy.Semantic proximity Read ↗

Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.Semantic proximity Read ↗

Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts.Semantic proximity Read ↗

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.Semantic proximity Read ↗

Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.Semantic proximity Read ↗

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