Small protein
Small proteins are a diverse fold class of proteins (usually <100 amino acids long).[1][2][3] Their tertiary structure is usually maintained by disulphide bridges,[4] metal ligands,[5] and or cofactors such as heme. Some small proteins serve important regulatory functions by direct interaction with certain enzymes and are therefore also an interesting tool for biotechnological applications in microorganisms. [6]
See also
References
- ^ Kihara D, Skolnick J (December 2003). "The PDB is a covering set of small protein structures". Journal of Molecular Biology. 334 (4): 793–802. doi:10.1016/j.jmb.2003.10.027. PMID 14636603.
- ^ Su M, Ling Y, Yu J, Wu J, Xiao J (December 2013). "Small proteins: untapped area of potential biological importance". Frontiers in Genetics. 4: 286. doi:10.3389/fgene.2013.00286. PMC 3864261. PMID 24379829.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Storz G, Wolf YI, Ramamurthi KS (2014-06-02). "Small proteins can no longer be ignored". Annual Review of Biochemistry. 83 (1): 753–77. doi:10.1146/annurev-biochem-070611-102400. PMC 4166647. PMID 24606146.
- ^ Cheek S, Krishna SS, Grishin NV (May 2006). "Structural classification of small, disulfide-rich protein domains". Journal of Molecular Biology. 359 (1): 215–37. doi:10.1016/j.jmb.2006.03.017. PMID 16618491.
- ^ Berg JM (April 1990). "Zinc fingers and other metal-binding domains. Elements for interactions between macromolecules". The Journal of Biological Chemistry. 265 (12): 6513–6. PMID 2108957.
- ^ Brandenburg F, Klähn S (2020). "Small but smart: On the diverse role of small proteins in the regulation of cyanobacterial metabolism". Life. 10 (12): 1–15. doi:10.3390/life10120322.
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