(Q36718622)

15 August 2017

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

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15 August 2017

2

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3

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15 August 2017

Merutka G

1

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15 August 2017

1 January 1995

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Journal of Biomolecular NMR

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5

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1

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15 August 2017

14-24

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https://scigraph.springernature.com/pub.10.1007/bf00227466

15 August 2017

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Carbon 13 nuclear magnetic resonance of pentapeptides of glycine containing central residues of methionine, proline, arginine, and lysine

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12 December 2020

Preferred spatial arrangement of the aromatic side chains in linear oligopeptides containing tyrosine

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12 December 2020

Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitor

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12 December 2020

Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Serine, Threonine, Aspartic and Glutamic Acids, Asparagine, and Glutamine

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12 December 2020

Secondary-structure dependent chemical shifts in proteins

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12 December 2020

Structural information from NMR secondary chemical shifts of peptide alpha C-H protons in proteins.

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12 December 2020

Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin

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12 December 2020

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

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12 December 2020

Solution structure of human calcitonin gene-related peptide by 1H NMR and distance geometry with restrained molecular dynamics.

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12 December 2020

Proton magnetic resonance studies in trifluoroethanol. Solvent mixtures as a means of delineating peptide protons

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12 December 2020

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

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12 December 2020

The 13C chemical shifts of amino acids in aqueous solution containing organic solvents: application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution

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12 December 2020

Protein conformation and proton nuclear-magnetic-resonance chemical shifts

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12 December 2020

Temperature dependence of amide proton chemical shifts: The secondary structures of gramicidin S and valinomycin

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12 December 2020

Defining solution conformations of small linear peptides

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12 December 2020

A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding

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12 December 2020

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin

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12 December 2020

NMR evidence for multiple conformations in a highly helical model peptide.

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12 December 2020

Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Aliphatic Amino Acids

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12 December 2020

Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments

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12 December 2020

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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12 December 2020

Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics.

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12 December 2020

The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale

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12 December 2020

Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix

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12 December 2020

Conformational studies of human Des-Trp1,Nle12 minigastrin in water-trifluoroethanol mixtures by proton NMR and circular dichroism

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12 December 2020

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin

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12 December 2020

Conformational requirement of signal sequences functioning in yeast: circular dichroism and 1H nuclear magnetic resonance studies of synthetic peptides

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12 December 2020

Structural characterization of monellin in the alcohol-denatured state by NMR: evidence for beta-sheet to alpha-helix conversion

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12 December 2020

Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal

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12 December 2020

Carbon-13 Magnetic Resonance Evaluation of Polypeptide Secondary Structure and Correlation with Proton Magnetic Resonance Studies

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12 December 2020

In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences

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12 December 2020

Identifiers

DOI

10.1007/BF00227466

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15 August 2017

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PubMed ID

7881270