Identification and quantification of proteoforms by mass spectrometry
A proteoform is a defined form of a protein derived from a given gene with a specific amino
acid sequence and localized post‐translational modifications. In top‐down proteomic …
acid sequence and localized post‐translational modifications. In top‐down proteomic …
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 …
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …
Tuning the flexibility of glycine-serine linkers to allow rational design of multidomain proteins
M Van Rosmalen, M Krom, M Merkx - Biochemistry, 2017 - ACS Publications
Flexible polypeptide linkers composed of glycine and serine are important components of
engineered multidomain proteins. We have previously shown that the conformational …
engineered multidomain proteins. We have previously shown that the conformational …
Are protein force fields getting better? A systematic benchmark on 524 diverse NMR measurements
Recent hardware and software advances have enabled simulation studies of protein
systems on biophysically relevant time scales, often revealing the need for improved force …
systems on biophysically relevant time scales, often revealing the need for improved force …
Exploring free-energy landscapes of intrinsically disordered proteins at atomic resolution using NMR spectroscopy
The last 15 years have seen a paradigm shift in our understanding of protein biochemistry,
with the realization that an unexpectedly high fraction of the human genome codes for …
with the realization that an unexpectedly high fraction of the human genome codes for …
Structure and energetics of the hydrogen-bonded backbone in protein folding
DW Bolen, GD Rose - Annu. Rev. Biochem., 2008 - annualreviews.org
We seek to understand the link between protein thermodynamics and protein structure in
molecular detail. A classical approach to this problem involves assessing changes in protein …
molecular detail. A classical approach to this problem involves assessing changes in protein …
Light-activated DNA binding in a designed allosteric protein
D Strickland, K Moffat… - Proceedings of the …, 2008 - National Acad Sciences
An understanding of how allostery, the conformational coupling of distant functional sites,
arises in highly evolvable systems is of considerable interest in areas ranging from cell …
arises in highly evolvable systems is of considerable interest in areas ranging from cell …
Describing intrinsically disordered proteins at atomic resolution by NMR
There is growing interest in the development of physical methods to study the
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …
Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering
The development of molecular descriptions of intrinsically disordered proteins (IDPs) is
essential for elucidating conformational transitions that characterize common …
essential for elucidating conformational transitions that characterize common …
Statistical coil model of the unfolded state: resolving the reconciliation problem
An unfolded state ensemble is generated by using a self-avoiding statistical coil model that
is based on backbone conformational frequencies in a coil library, a subset of the Protein …
is based on backbone conformational frequencies in a coil library, a subset of the Protein …