Over the past decade, the Rosetta biomolecular modeling suite has informed diverse
biological questions and engineering challenges ranging from interpretation of low …

On the occasion of their fiftieth birthday, it is opportune to review the first half century of
Ramachandran plots. In the present review, some of the most relevant aspects of this fifty …

Cryo-EM has revealed the structures of many challenging yet exciting macromolecular
assemblies at near-atomic resolution (3–4.5 Å), providing biological phenomena with …

Development of the AMOEBA (atomic multipole optimized energetics for biomolecular
simulation) force field for proteins is presented. The current version (AMOEBA-2013) utilizes …

Over the last thirty years the unfolded state of proteins has attracted considerable interest
owing to the discovery of intrinsically disordered proteins which perform a plethora of …

Previous analyses of the complementarity-determining regions (CDRs) of antibodies have
focused on a small number of “canonical” conformations for each loop. This is primarily the …

We present the AMBER ff15ipq force field for proteins, the second-generation force field
developed using the Implicitly Polarized Q (IPolQ) scheme for deriving implicitly polarized …

Random coil chemical shifts are necessary for secondary chemical shift analysis, which is
the main NMR method for identification of secondary structure in proteins. One of the largest …

Secondary chemical shift analysis is the main NMR method for detection of transiently
formed secondary structure in intrinsically disordered proteins. The quality of the secondary …

Chemical shifts contain important site-specific information on the structure and dynamics of
proteins. Deviations from statistical average values, known as random coil chemical shifts …