Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites

A Propensity Scale for Type II Polyproline Helices (PPII): Aromatic Amino Acids in Proline-Rich Sequences Strongly Disfavor PPII Due to Proline–Aromatic Interactions

(2012) Alaina M. Brown et al.   BIOCHEMISTRY

MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins

(2012) Fatemeh Miri Disfani et al.   BIOINFORMATICS

Conformational Dynamics of Titin PEVK Explored with FRET Spectroscopy

(2012) Tamás Huber et al.   BIOPHYSICAL JOURNAL

Direct Evidence for CH···π Interaction Mediated Stabilization of Pro-cisPro Bond in Peptides with Pro-Pro-Aromatic motifs

(2012) Himal K. Ganguly et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

A Statistical Analysis of the PPII Propensity of Amino Acid Guests in Proline-Rich Peptides

(2011) Mahmoud Moradi et al.   BIOPHYSICAL JOURNAL

Multi-Scale Sequence Correlations Increase Proteome Structural Disorder and Promiscuity

(2011) Ariel Afek et al.   JOURNAL OF MOLECULAR BIOLOGY

Populations of the three major backbone conformations in 19 amino acid dipeptides

(2011) Joze Grdadolnik et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Phosphorylation alters backbone conformational preferences of serine and threonine peptides

(2011) Su-Yeon Kim et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins

(2011) Kwang-Im Oh et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be

(2010) Christian Schaefer et al.   BIOINFORMATICS

Phosphorylated and Nonphosphorylated Serine and Threonine Residues Evolve at Different Rates in Mammals

(2010) S. C.-C. Chen et al.   MOLECULAR BIOLOGY AND EVOLUTION

Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

(2010) A. H. Mao et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria

(2010) Silvia Domingo Köhler et al.   PROTEIN SCIENCE

Comparing Models of Evolution for Ordered and Disordered Proteins

(2009) C. J. Brown et al.   MOLECULAR BIOLOGY AND EVOLUTION

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

(2009) Da Wei Huang et al.   Nature Protocols

The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins

(2008) D. A. C. Beck et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder

(2008) Andrew Campen et al.   PROTEIN AND PEPTIDE LETTERS

Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain

(2008) Steven T. Whitten et al.   PROTEIN SCIENCE

A novel method reveals that solvent water favors polyproline II over β-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA)

(2004) Patrick J. Fleming et al.   PROTEIN SCIENCE