(Q33943720)

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Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices

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Europe PubMed Central

PubMed publication ID

30 July 2017

Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

S T Thomas

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

V V Loladze

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

G I Makhatadze

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

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publication date

4 September 2001

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Europe PubMed Central

PubMed publication ID

30 July 2017

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

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Europe PubMed Central

PubMed publication ID

30 July 2017

98

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Europe PubMed Central

PubMed publication ID

30 July 2017

19

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

10670-10675

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain

1 reference

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Heat capacity changes upon burial of polar and nonpolar groups in proteins

1 reference

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To charge or not to charge?

1 reference

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Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine

1 reference

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Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities

1 reference

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Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface

1 reference

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Interaction between water and polar groups of the helix backbone: an important determinant of helix propensities

1 reference

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Stability and folding of domain proteins

1 reference

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Deciphering rules of helix stability in peptides

1 reference

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Anion binding to the ubiquitin molecule

1 reference

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How to measure and predict the molar absorption coefficient of a protein

1 reference

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5 July 2018

Energetics of protein structure.

1 reference

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Amino-acid substitutions in a surface turn modulate protein stability

1 reference

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Structural basis of amino acid alpha helix propensity

1 reference

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Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

5 July 2018

Structural and genetic analysis of protein stability

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

5 July 2018

Primary structure effects on peptide group hydrogen exchange

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

5 July 2018

Rules for alpha-helix termination by glycine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

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Correction of light‐scattering errors in spectrophotometric protein determinations

1 reference

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Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid

1 reference

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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

1 reference

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5 July 2018

Amino acid preferences for specific locations at the ends of alpha helices

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

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Recurring loop motif in proteins that occurs in right-handed and left-handed forms. Its relationship with alpha-helices and beta-bulge loops

1 reference

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Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

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Helix signals in proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=58524

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Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme

1 reference

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Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range

1 reference

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On alpha-helices terminated by glycine. 1. Identification of common structural features.

1 reference

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On α-helices terminated by glycine

1 reference

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Helix stop signals in proteins and peptides: the capping box

1 reference

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Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.191381798

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Contribution of the 30/36 hydrophobic contact at the C-terminus of the alpha-helix to the stability of the ubiquitin molecule

1 reference

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Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability

1 reference

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Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect

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Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins

1 reference

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Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility

1 reference

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Alpha-helix-forming propensities in peptides and proteins

1 reference

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The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes

1 reference

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Identifiers

10.1073/PNAS.191381798

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

2001PNAS...9810670T

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

ResearchGate publication ID

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