Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins-Reference-Cited by-同舟云学术

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Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins

Published:2012-02-22 Issue: Volume: Page:131-158
ISSN:
Container-title:Protein and Peptide Folding, Misfolding, and Non-Folding
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Author:

Avbelj Franc

Publisher

John Wiley & Sons, Inc.

Reference160 articles.

1. Seeding protein folding;Baldwin;Trends Biochem Sci,1986

2. Thermodynamic cycles as probes of structure in unfolded proteins;McGee;Biochemistry,1996

3. Denatured states of proteins;Dill;Annu Rev Biochem,1991

4. Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride;Logan;J Mol Biol,1994

5. Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional NMR spectroscopy;Frank;Protein Sci,1995

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1. The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins;Physical Chemistry Chemical Physics;2023

2. Short Peptides as Predictors for the Structure of Polyarginine Sequences in Disordered Proteins;2020-09-17

3. Probing conformational propensities of histidine in different protonation states of the unblocked glycyl-histidyl-glycine peptide by vibrational and NMR spectroscopy;Journal of Raman Spectroscopy;2016-02-24

4. Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor Interactions between Unlike Residues;Chemistry - A European Journal;2015-02-26

5. Role of Enthalpy–Entropy Compensation Interactions in Determining the Conformational Propensities of Amino Acid Residues in Unfolded Peptides.;The Journal of Physical Chemistry B;2014-01-27

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