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Effects of Fluorophore Attachment on Protein Conformation and Dynamics Studied by spFRET and NMR Spectroscopy. [PDF]

open access: yesChemistry, 2017
Sánchez-Rico C   +4 more
europepmc   +1 more source
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Conformational spectra — probing protein conformational changes

Biophysical Chemistry, 1999
Stafford [Biophys. J. 17 (1996) MP452] has shown that it is possible, using the analytical ultracentrifuge in sedimentation velocity mode, to calculate the molecular weights of proteins with a precision of approximately 5%, by fitting Gaussian distributions to g(s*) profiles so long as partial specific volume and the radial position of the meniscus are
N, Errington, O, Byron, A J, Rowe
openaire   +2 more sources

Conformation spaces of proteins

Proteins: Structure, Function, and Bioinformatics, 2001
We report a simple method for measuring the accessible conformational space explored by an ensemble of protein structures. The method is useful for diverse ensembles derived from molecular dynamics trajectories, molecular modeling, and molecular structure determinations. It can be used to examine a wide range of time scales.
D C, Sullivan, I D, Kuntz
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Protein conformational prediction

Trends in Biochemical Sciences, 1989
The prediction of the secondary and tertiary structure of globular and membrane proteins is reviewed. Prospects are encouraging for future developments, but present algorithms require cautious interpretation.
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Exploring Protein Conformational Diversity

2018
The native state of proteins is composed of conformers in dynamical equilibrium. In this chapter, different issues related to conformational diversity are explored using a curated and experimentally based database called CoDNaS (Conformational Diversity in the Native State).
Monzon, Alexander Miguel   +3 more
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Lethal protein conformations

Trends in Biochemical Sciences, 1980
A discussion of how snake venom neurotoxins may imitate the structures of arrow poisons and chemical transmitters in order to paralyse and ...
M.J. Dufton, R.C. Hider
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Conformational stability of globular proteins

Trends in Biochemical Sciences, 1990
The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
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