Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Utility of B-Factors in Protein Science: Interpreting Rigidity, Flexibility, and Internal Motion and Engineering Thermostability


Reetz,  Manfred T.
Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Chemistry Department, Philipps-University;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Sun, Z., Liu, Q., Qu, G., Feng, Y., & Reetz, M. T. (2019). Utility of B-Factors in Protein Science: Interpreting Rigidity, Flexibility, and Internal Motion and Engineering Thermostability. Chemical Reviews, 119(3), 1626-1665. doi:10.1021/acs.chemrev.8b00290.

Cite as: https://hdl.handle.net/21.11116/0000-0003-3F9C-8
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-ray or neutron scattering caused by thermal motion. This review begins with analyses of early protein studies which suggested that B-factors, available from the Protein Data Bank, can be used to identify the flexibility of atoms, side chains, or even whole regions. This requires a technique for obtaining normalized B-factors. Since then the exploitation of B-factors has been extensively elaborated and applied in a variety of studies with quite different goals, all having in common the identification and interpretation of rigidity, flexibility, and/or internal motion which are crucial in enzymes and in proteins in general. Importantly, this review includes a discussion of limitations and possible pitfalls when using B-factors. A second research area, which likewise exploits B-factors, is also reviewed, namely, the development of the so-called B-FIT-directed evolution method for increasing the thermostability of enzymes as catalysts in organic chemistry and biotechnology. In both research areas, a maximum of structural and mechanistic insights is gained when B-factor analyses are combined with other experimental and computational techniques.