Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides. (Q36820079)

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scientific article published on July 1996

Language	Label	Description	Also known as
English	Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides.	scientific article published on July 1996

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8810526%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides (English)

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8810526%20AND%20SRC:MED&resulttype=core&format=json

19 October 2019

Frank D Sönnichsen

8

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19 October 2019

author name string

S Rothemund

1

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19 October 2019

H Weisshoff

2

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19 October 2019

M Beyermann

3

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19 October 2019

E Krause

4

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19 October 2019

M Bienert

5

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19 October 2019

C Mügge

6

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19 October 2019

B D Sykes

7

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19 October 2019

publication date

1 July 1996

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19 October 2019

Journal of Biomolecular NMR

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19 October 2019

8

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19 October 2019

1

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19 October 2019

93-97

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19 October 2019

Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies.

1 reference

https://api.crossref.org/works/10.1007%2FBF00198143

21 January 2018

'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.

1 reference

https://pubmed.ncbi.nlm.nih.gov/8810526

12 December 2020

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Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/8810526

12 December 2020

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Conformations of the repeat peptides of elastin in solution: an application of proton and carbon-13 magnetic resonance to the determination of polypeptide secondary structure

1 reference

https://pubmed.ncbi.nlm.nih.gov/8810526

12 December 2020

based on heuristic

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Protein conformation and proton nuclear-magnetic-resonance chemical shifts

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Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach

1 reference

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12 December 2020

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

1 reference

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Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysis

1 reference

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12 December 2020

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Circular dichroism studies of isoleucine oligopeptides in solution

1 reference

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12 December 2020

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

1 reference

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12 December 2020

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

1 reference

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12 December 2020

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Three-dimensional structure of membrane and surface proteins

1 reference

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12 December 2020

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Structure effects of double D-amino acid replacements: a nuclear magnetic resonance and circular dichroism study using amphipathic model helices.

1 reference

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Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn

1 reference

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12 December 2020

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Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

1 reference

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12 December 2020

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