The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations (Q35800301)

10 August 2017

The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations (English)

1 reference

Reinhard Schweitzer-Stenner

10 August 2017

series ordinal

1

object named as

Reinhard Schweitzer-Stenner

1 reference

10 August 2017

Thomas J Measey

2

1 reference

PMC publication ID

1871840

10 August 2017

language of work or name

English

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publication date

6 April 2007

1 reference

Proceedings of the National Academy of Sciences of the United States of America

10 August 2017

1 reference

10 August 2017

104

1 reference

10 August 2017

16

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10 August 2017

6649-6654

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Conformations of alanine-based peptides in water probed by FTIR, Raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy.

10 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Polyproline II helix conformation in a proline-rich environment: a theoretical study

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Stereochemistry of polypeptide chain configurations

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: Distributions of phi

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Structural composition of betaI- and betaII-proteins

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Is polyproline II a major backbone conformation in unfolded proteins?

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Intrinsically disordered protein

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

27 July 2018

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

27 July 2018

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Prediction of protein conformation

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins

27 July 2018

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

27 July 2018

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Unusually stable helix formation in short alanine-based peptides

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1871840

Conformation of the backbone in unfolded proteins.

27 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Tripeptides adopt stable structures in water. A combined polarized visible Raman, FTIR, and VCD spectroscopy study

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Reconciling observations of sequence-specific conformational propensities with the generic polymeric behavior of denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Short sequences of non-proline residues can adopt the polyproline II helical conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Single peptide bonds exhibit poly(pro)II ("random coil") circular dichroism spectra

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Polyproline II structure in a sequence of seven alanine residues.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Helix-coil transition of alanine peptides in water: force field dependence on the folded and unfolded structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Unusual compactness of a polyproline type II structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Conformational distribution of a 14-residue peptide in solution: a fluorescence resonance energy transfer study.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Tripeptides with ionizable side chains adopt a perturbed polyproline II structure in water

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

The conformation of tetraalanine in water determined by polarized Raman, FT-IR, and VCD spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Ab initio-based exciton model of amide I vibrations in peptides: definition, conformational dependence, and transferability.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Abeta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Structure of the Amide I Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Amide I vibrational circular dichroism of dipeptide: Conformation dependence and fragment analysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Conformational analysis of XA and AX dipeptides in water by electronic circular dichroism and 1H NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Is polyproline II helix the killer conformation? a raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme 1 1Edited by A. R. Fersht

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR Measurements

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Structure of Poly-L-Proline

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0700006104

Circular dichroism of poly-L-proline in an unordered conformation

21 January 2018

1 reference

12 December 2020

On the relevance of non-random polypeptide conformations for protein folding

1 reference

12 December 2020

Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides

1 reference

12 December 2020

A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins

1 reference

12 December 2020

Salmon calcitonin and amyloid beta: two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states

1 reference

12 December 2020

Side chain dependence of intensity and wavenumber position of amide I' in IR and visible Raman spectra of XA and AX dipeptides

1 reference

12 December 2020

Unfolding of alanine-based peptides using electron spin resonance distance measurements

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.0700006104

1 reference

10 August 2017

0 references

1 reference

PMC publication ID

1871840

10 August 2017

PubMed publication ID

17416675

1 reference

PMC publication ID

1871840