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A molecular-weight size marker, also referred to as a protein ladder, DNA ladder, or RNA ladder, is a set of standards that are used to identify the approximate size of a molecule run on a gel during electrophoresis, using the principle that molecular weight is inversely proportional to migration rate through a gel matrix.
A more sophisticated analysis known as 'composition-gradient static (or multi-angle) light scattering' (CG-SLS or CG-MALS) is an important class of methods to investigate protein–protein interactions, colligative properties, and other macromolecular interactions as it yields, in addition to size and molecular weight, information on the ...
Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.
The Young's modulus of a single protein can be found through molecular dynamics simulation. Using either atomistic force-fields, such as CHARMM or GROMOS, or coarse-grained forcefields like Martini, [121] a single protein molecule can be stretched by a uniaxial force while the resulting extension is recorded in order to calculate the strain.
The technique is based on measuring the change in apparent size (hydrodynamic radius) of a selective ligand when interacting with the analyte of interest. A FIDA assay works in complex solutions (e.g. plasma [18]), and provides information regarding analyte concentration, affinity constants, molecular size and binding kinetics. A single assay ...
Protein structures range in size from tens to several thousand amino acids. [2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.
The Stokes radius or Stokes–Einstein radius of a solute is the radius of a hard sphere that diffuses at the same rate as that solute. Named after George Gabriel Stokes, it is closely related to solute mobility, factoring in not only size but also solvent effects.
Shibuya T (2009). "Searching Protein 3-D Structures in Linear Time." Proc. 13th Annual International Conference on Research in Computational Molecular Biology (RECOMB 2009), LNCS 5541:1–15. Damm KL, Carlson HA (2006). "Gaussian-Weighted RMSD Superposition of Proteins: A Structural Comparison for Flexible Proteins and Predicted Protein ...