---
_id: '8489'
abstract:
- lang: eng
  text: Structure elucidation of proteins by either NMR or X‐ray crystallography often
    requires the screening of a large number of samples for promising protein constructs
    and optimum solution conditions. For large‐scale screening of protein samples
    in solution, robust methods are needed that allow a rapid assessment of the folding
    of a polypeptide under diverse sample conditions. Here we present HET‐SOFAST NMR,
    a highly sensitive new method for semi‐quantitative characterization of the structural
    compactness and heterogeneity of polypeptide chains in solution. On the basis
    of one‐dimensional 1H HET‐SOFAST NMR data, obtained on well‐folded, molten globular,
    partially‐ and completely unfolded proteins, we define empirical thresholds that
    can be used as quantitative benchmarks for protein compactness. For 15N‐enriched
    protein samples, two‐dimensional 1H‐15N HET‐SOFAST correlation spectra provide
    site‐specific information about the structural heterogeneity along the polypeptide
    chain.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Vincent
  full_name: Forge, Vincent
  last_name: Forge
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Schanda P, Forge V, Brutscher B. HET-SOFAST NMR for fast detection of structural
    compactness and heterogeneity along polypeptide chains. <i>Magnetic Resonance
    in Chemistry</i>. 2006;44(S1):S177-S184. doi:<a href="https://doi.org/10.1002/mrc.1825">10.1002/mrc.1825</a>
  apa: Schanda, P., Forge, V., &#38; Brutscher, B. (2006). HET-SOFAST NMR for fast
    detection of structural compactness and heterogeneity along polypeptide chains.
    <i>Magnetic Resonance in Chemistry</i>. Wiley. <a href="https://doi.org/10.1002/mrc.1825">https://doi.org/10.1002/mrc.1825</a>
  chicago: Schanda, Paul, Vincent Forge, and Bernhard Brutscher. “HET-SOFAST NMR for
    Fast Detection of Structural Compactness and Heterogeneity along Polypeptide Chains.”
    <i>Magnetic Resonance in Chemistry</i>. Wiley, 2006. <a href="https://doi.org/10.1002/mrc.1825">https://doi.org/10.1002/mrc.1825</a>.
  ieee: P. Schanda, V. Forge, and B. Brutscher, “HET-SOFAST NMR for fast detection
    of structural compactness and heterogeneity along polypeptide chains,” <i>Magnetic
    Resonance in Chemistry</i>, vol. 44, no. S1. Wiley, pp. S177–S184, 2006.
  ista: Schanda P, Forge V, Brutscher B. 2006. HET-SOFAST NMR for fast detection of
    structural compactness and heterogeneity along polypeptide chains. Magnetic Resonance
    in Chemistry. 44(S1), S177–S184.
  mla: Schanda, Paul, et al. “HET-SOFAST NMR for Fast Detection of Structural Compactness
    and Heterogeneity along Polypeptide Chains.” <i>Magnetic Resonance in Chemistry</i>,
    vol. 44, no. S1, Wiley, 2006, pp. S177–84, doi:<a href="https://doi.org/10.1002/mrc.1825">10.1002/mrc.1825</a>.
  short: P. Schanda, V. Forge, B. Brutscher, Magnetic Resonance in Chemistry 44 (2006)
    S177–S184.
date_created: 2020-09-18T10:13:42Z
date_published: 2006-07-06T00:00:00Z
date_updated: 2021-01-12T08:19:37Z
day: '06'
doi: 10.1002/mrc.1825
extern: '1'
intvolume: '        44'
issue: S1
language:
- iso: eng
month: '07'
oa_version: None
page: S177-S184
publication: Magnetic Resonance in Chemistry
publication_identifier:
  issn:
  - 0749-1581
  - 1097-458X
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: HET-SOFAST NMR for fast detection of structural compactness and heterogeneity
  along polypeptide chains
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 44
year: '2006'
...