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Utility of B-factors in protein science: interpreting rigidity, flexibility, and internal motion and engineering thermostability
Z Sun, Q Liu, G Qu, Y Feng, MT Reetz - Chemical reviews, 2019 - ACS Publications
The term B-factor, sometimes called the Debye–Waller factor, temperature factor, or atomic
displacement parameter, is used in protein crystallography to describe the attenuation of X …
displacement parameter, is used in protein crystallography to describe the attenuation of X …
Classification of intrinsically disordered regions and proteins
Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation
Intrinsically disordered proteins and protein regions (IDPs/IDRs) exist without a single well-
defined conformation. They carry out important biological functions with multifaceted roles …
defined conformation. They carry out important biological functions with multifaceted roles …
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding
The structural states of proteins include ordered globular domains as well as intrinsically
disordered protein regions that exist as highly flexible conformational ensembles in …
disordered protein regions that exist as highly flexible conformational ensembles in …
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …
proteins. For the majority of human proteins that contain intrinsically disordered regions …
In situ analysis of osmolyte mechanisms of proteome thermal stabilization
M Pepelnjak, B Velten, N Näpflin, T von Rosen… - Nature Chemical …, 2024 - nature.com
Organisms use organic molecules called osmolytes to adapt to environmental conditions. In
vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are …
vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are …
DISOPRED3: precise disordered region predictions with annotated protein-binding activity
Motivation: A sizeable fraction of eukaryotic proteins contain intrinsically disordered regions
(IDRs), which act in unfolded states or by undergoing transitions between structured and …
(IDRs), which act in unfolded states or by undergoing transitions between structured and …
Intrinsically disordered proteins and intrinsically disordered protein regions
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
[HTML][HTML] Protein stability: a crystallographer's perspective
Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …
industries, in addition to being a daily consideration for academic researchers studying …
Sixty-five years of the long march in protein secondary structure prediction: the final stretch?
Protein secondary structure prediction began in 1951 when Pauling and Corey predicted
helical and sheet conformations for protein polypeptide backbone even before the first …
helical and sheet conformations for protein polypeptide backbone even before the first …