Design of folded peptides

J Venkatraman, SC Shankaramma… - Chemical reviews, 2001 - ACS Publications
The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins

FX Theillet, L Kalmar, P Tompa, KH Han… - Intrinsically …, 2013 - Taylor & Francis
A significant fraction of every proteome is occupied by biologically active proteins that do not
form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and …

Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs

A Senes, DE Engel, WF DeGrado - Current opinion in structural biology, 2004 - Elsevier
Helical integral membrane proteins share several structural determinants that are widely
conserved across their universe. The discovery of common motifs has furthered our …

De novo design and structural characterization of proteins and metalloproteins

WF DeGrado, CM Summa, V Pavone… - Annual review of …, 1999 - annualreviews.org
▪ Abstract De novo protein design has recently emerged as an attractive approach for
studying the structure and function of proteins. This approach critically tests our …

[HTML][HTML] The interrelationships of side-chain and main-chain conformations in proteins

P Chakrabarti, D Pal - Progress in biophysics and molecular biology, 2001 - Elsevier
The accurate determination of a large number of protein structures by X-ray crystallography
makes it possible to conduct a reliable statistical analysis of the distribution of the main …

Venom composition and strategies in spiders: is everything possible?

L Kuhn-Nentwig, R Stöcklin, W Nentwig - Advances in insect physiology, 2011 - Elsevier
This review on all spider venom components known by the end of 2010 bases on 1618
records for venom compounds from 174 spider species (= 0.41% of all known species) …

The role of α‐, 310‐, and π‐helix in helix→coil transitions

R Armen, DOV Alonso, V Daggett - Protein Science, 2003 - Wiley Online Library
The conformational equilibrium between 310‐and α‐helical structure has been studied via
high‐resolution NMR spectroscopy by Millhauser and coworkers using the MW peptide Ac …

Prevalence and nonrandom distribution of exonic mutations in interferon regulatory factor 6 in 307 families with Van der Woude syndrome and 37 families with …

RLL de Lima, SA Hoper, M Ghassibe, ME Cooper… - Genetics in …, 2009 - nature.com
Purpose: Interferon regulatory factor 6 encodes a member of the IRF family of transcription
factors. Mutations in interferon regulatory factor 6 cause Van der Woude and popliteal …

How different are structurally flexible and rigid binding sites? Sequence and structural features discriminating proteins that do and do not undergo conformational …

K Gunasekaran, R Nussinov - Journal of molecular biology, 2007 - Elsevier
Proteins are dynamic molecules and often undergo conformational change upon ligand
binding. It is widely accepted that flexible loop regions have a critical functional role in …

Stereochemical control of peptide folding

R Kaul, P Balaram - Bioorganic & medicinal chemistry, 1999 - Elsevier
Stereochemically constrained amino acid residues that strongly favour specific backbone
conformations may be used to nucleate and stabilize specific secondary structures in …