Polyproline-II helix in proteins: structure and function

AA Adzhubei, MJE Sternberg, AA Makarov - Journal of molecular biology, 2013 - Elsevier
The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

A fresh look at the Ramachandran plot and the occurrence of standard structures in proteins

SA Hollingsworth, PA Karplus - 2010 - degruyter.com
The Ramachandran plot is among the most central concepts in structural biology, seen in
publications and textbooks alike. However, with the increasing numbers of known protein …

A common structural motif incorporating a cystine knot and a triple‐stranded β‐sheet in toxic and inhibitory polypeptides

PK Pallaghy, RS Norton, KJ Nielsen… - Protein Science, 1994 - Wiley Online Library
A common structural motif consisting of a cystine knot and a small triple‐stranded β‐sheet
has been defined from comparison of the 3‐dimensional structures of the polypeptides ω …

Left-handed polyproline II helices commonly occur in globular proteins

AA Adzhubei, MJE Sternberg - Journal of molecular biology, 1993 - Elsevier
The main-chain conformations of 80 proteins were analyzed to identify helical structures that
commonly occur but do not fall into the known classes of α-helix, 3 10-helix and β-sheet. The …

Statistical clustering techniques for the analysis of long molecular dynamics trajectories: analysis of 2.2-ns trajectories of YPGDV

ME Karpen, DJ Tobias, CL Brooks III - Biochemistry, 1993 - ACS Publications
The microscopic interactions and mechanisms leading to nascent protein folding events are
generally unknown. While such short time-scale events are difficult to study experimentally …

[HTML][HTML] Solution structure and dynamics of biomolecules from Raman optical activity

LD Barron, L Hecht, EW Blanch, AF Bell - Progress in Biophysics and …, 2000 - Elsevier
Raman optical activity (ROA) measures vibrational optical activity by means of a small
difference in the intensity of Raman scattering from chiral molecules in right and left …

Solution structure of native proteins with irregular folds from Raman optical activity

E Smyth, CD Syme, EW Blanch, L Hecht… - Biopolymers …, 2001 - Wiley Online Library
Raman optical activity (ROA) spectra have been measured for the proteins hen phosvitin,
yeast invertase, bovine α‐casein, soybean Bowman–Birk protease inhibitor, and rabbit Cd7 …

Unfolded proteins studied by Raman optical activity

LD Barron, EW Blanch, L Hecht - Advances in Protein Chemistry, 2002 - Elsevier
Publisher Summary To understand the behavior of unfolded proteins it is necessary to
employ experimental techniques able to discriminate between the dynamic true random coil …

Evolutionary analysis of polyproline motifs in Escherichia coli reveals their regulatory role in translation

F Qi, M Motz, K Jung, J Lassak… - PLoS computational …, 2018 - journals.plos.org
Translation of consecutive prolines causes ribosome stalling, which is alleviated but cannot
be fully compensated by the elongation factor P. However, the presence of polyproline …

Structure of coiled β‐β‐hairpins and β‐β‐corners

AV Efimov - FEBS letters, 1991 - Wiley Online Library
Two types of super‐secondary structure, coiled β‐β‐hairpins and β‐β‐corners, are
considered in this paper. A β‐β‐corner can be represented as a long β‐β‐hairpin folded …