Engineering the dynamic properties of protein networks through sequence variation

LJ Dooling, DA Tirrell - ACS central science, 2016 - ACS Publications
The dynamic behavior of macromolecular networks dominates the mechanical properties of
soft materials and influences biological processes at multiple length scales. In hydrogels …

N-terminal aliphatic residues dictate the structure, stability, assembly, and small molecule binding of the coiled-coil region of cartilage oligomeric matrix protein

SK Gunasekar, M Asnani, C Limbad… - Biochemistry, 2009 - ACS Publications
The coiled-coil domain of cartilage oligomeric matrix protein (COMPcc) assembles into a
homopentamer that naturally recognizes the small molecule 1, 25-dihydroxyvitamin D3 (vit …

Assembly of bioinspired helical protein fibers

SK Gunasekar, JS Haghpanah… - Polymers for Advanced …, 2008 - Wiley Online Library
Advances in protein and peptide technologies not only enable the study of basic folding and
function of natural structures but also the design of novel scaffolds with the ability to form …

Engineered multivalent self-assembled binder protein against SARS-CoV-2 RBD

D Britton, K Punia, F Mahmoudinobar, T Tada… - Biochemical …, 2022 - Elsevier
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a global
pandemic since December 2019, and with it, a push for innovations in rapid testing and …

The open reading frame III product of cauliflower mosaic virus forms a tetramer through a N-terminal coiled-coil

D Leclerc, L Burri, AV Kajava, JL Mougeot… - Journal of Biological …, 1998 - ASBMB
The open reading frame III product of cauliflower mosaic virus is a protein of 15 kDa (p15)
that is essential for the virus life cycle. It was shown that the 34 N-terminal amino acids are …

Energetic determinants of oligomeric state specificity in coiled coils

J Ramos, T Lazaridis - Journal of the American Chemical Society, 2006 - ACS Publications
The coiled coil is one of the simplest and best-studied protein structural motifs, consisting of
two to five helices wound around each other. Empirical rules have been established on the …

Shift of fibril‐forming ability of the designed α‐helical coiled‐coil peptides into the physiological pH region

TN Melnik, V Villard, V Vasiliev, G Corradin… - Protein …, 2003 - academic.oup.com
Recently, we designed a short α‐helical fibril‐forming peptide (αFFP) that can form α‐helical
nanofibrils at acid pH. The non‐physiological conditions of the fibril formation hamper …

Programming Molecular Association and Viscoelastic Behavior in Protein Hydrogels

LJ Dooling - 2016 - thesis.library.caltech.edu
Recombinant artificial proteins contain genetically encoded information that specifies their
assembly into higher order structures by physical or chemical cross-linking as well as elastic …