P. M. M. Schrooyen, P. J. Dijkstra, R. C. Oberthur, A. Bantjes and J. Feijen, J. Colloid Interf. Sci., 2001, 240, 30 CrossRef CAS. Jia JR, Yao JB, Liu JY, Liu YB. Application of dissolved wool keratin in anti-pilling processing. Key Eng Mater. 2015;671:53–8. Yamauchi K, Yamauchi A, Kusunoki T, Kohda A, Konishi Y. Preparation of stable aqueous solution of keratins, and physiochemical and biodegradational properties of films. J Biomed Mater Res. 1996;31:439–44. The human genome has 54 functional annotated Keratin genes, 28 are in the Keratin type 1 family, and 26 are in the Keratin type 2 family. [19] Keratin (high molecular weight) in bile duct cell and oval cells of horse liver.

Omary, M. Bishr; Ku, Nam-On; Strnad, Pavel; Hanada, Shinichiro (1 July 2009). "Toward unraveling the complexity of simple epithelial keratins in human disease". Journal of Clinical Investigation. 119 (7): 1794–1805. doi: 10.1172/JCI37762. PMC 2701867. PMID 19587454. Find sources: "Keratin"– news · newspapers · books · scholar · JSTOR ( January 2022) ( Learn how and when to remove this template message) Rajkhowa R, Zhou Q, Tsuzuki T, Morton DAV, Wang X. Ultrafine wool powders and their bulk properties. Powder Technol. 2012;224:183–8. Buchanan JH. A cystine-rich protein fraction from oxidized α-keratin. Biochem J. 1977;167(2):489–91.

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The human genome encodes 54 functional keratin genes, located in two clusters on chromosomes 12 and 17. This suggests that they originated from a series of gene duplications on these chromosomes. [13] Type II: The other 26 kinds of keratins in your body are type II. Of those, 20 are skin cell keratins, and six are hair keratins. They consist of basic-neutral, high-weight proteins. Their basic-neutral pH helps balance type I keratins and govern cell activity. Ingredients: Creatine monohydrate should always be the key ingredient, but some supplements may include other additive. Opt for a single-ingredient, pure creatine whenever possible.

Zhang ZL, Nie Y, Zhang QS, Liu X, Tu WH, Zhang XP, Zhang SJ. Quantitative change in disulfide bonds and microstructure variation of regenerated wool keratin from various ionic liquids. ACS Sustain Chem Eng. 2017;5(3):2614–22.

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Hanukoglu, Israel; Ezra, Liora (January 2014). "Proteopedia entry: Coiled-coil structure of keratins: Multimedia in Biochemistry and Molecular Biology Education". Biochemistry and Molecular Biology Education. 42 (1): 93–94. doi: 10.1002/bmb.20746. PMID 24265184. S2CID 30720797. As expected, soft viscoelastic fibers are difficult to mill into nano-powder. Thus, the pretreatment for wool fiber is an effective manner to produce nanoscale powder. Cheng et al. [ 25] developed a pretreatment approach for wool fibers using a hydrogen peroxide solution. This included three main stages, as indicated by its name. First stage In collaboration with creatine expert Jose Antonio, PhD, C.S.C.S., a professor in the Department of of Exercise and Sport Science at Nova Southeastern University in Fort Lauderdale, Fl., Men's Health fitness editors evaluated more than two dozen creatine products. Here's what we've found: look for supplements certified by NSF or Informed Choice, and choose pure creatine monohydrate with 5 grams per serving—no fillers or extra ingredients. The Global Info Research report includes an overview of the development of the Keratin Powder industry chain, the market status of Pharmaceutical (α-Keratin Powder, β-Keratin Powder), Cosmetic (α-Keratin Powder, β-Keratin Powder), and key enterprises in developed and developing market, and analysed the cutting-edge technology, patent, hot applications and market trends of Keratin Powder.

It has been proposed that keratins can be divided into 'hard' and 'soft' forms, or ' cytokeratins' and 'other keratins'. [ clarification needed] [ dubious – discuss] That model is now understood to be correct. A new nuclear addition in 2006 to describe keratins takes this into account. [14] Fraser, R.D.B. (1972). Keratins: Their composition, structure and biosynthesis. Bannerstone House: Charles C Thomas. pp.3–6. ISBN 978-0-398-02283-9.

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Aluigi. Wool keratin nanofibres for copper (II) adsorption. J Biobased Mater Bioenergy. 2012;6(2):230–6. The first sequences of keratins were determined by Israel Hanukoglu and Elaine Fuchs (1982, 1983). [16] [17] These sequences revealed that there are two distinct but homologous keratin families, which were named type I and type II keratins. [17] By analysis of the primary structures of these keratins and other intermediate filament proteins, Hanukoglu and Fuchs suggested a model in which keratins and intermediate filament proteins contain a central ~310 residue domain with four segments in α-helical conformation that are separated by three short linker segments predicted to be in beta-turn conformation. [17] This model has been confirmed by the determination of the crystal structure of a helical domain of keratins. [18] Type 1 and 2 Keratins [ edit ] Large wool particles were pulverized with an ultrasonic crusher to obtain wool powder with a diameter of 0.1–7 μm. Third stage Works well with: “Since keratin is a naturally occurring protein with smoothing benefits that minimize frizz and make hair glossy and manageable, other products can reinforce the benefits of keratin,” Steinmetz says, noting that natural oils like argan can help add moisture to damaged hair, and silicone-based finishing products can help further smooth the hair's surface.” The major force that keeps the coiled-coil structure is hydrophobic interactions between apolar residues along the keratins helical segments. [21]

Naik R, Wen G, Ms D, Hureau S, Uedono A, Wang X, Liu X, Cookson PG, Smith SV. Metal ion binding properties of novel wool powders. J Appl Polym Sci. 2010;115(3):1642–50. Ferroni C, Sotgiu G, Sagnella A, Varchi G, Guerrini A, Giuri D, Polo E, Orlandi VT, Marras E, Gariboldi M, Monti E, Aluigi A. Wool keratin 3D scaffolds with light-triggered antimicrobial activity. Biomacromolecules. 2016;17(9):2882–90. Gan L, Guo H, Xiao Z, Jia Z, Yang H, Sheng D, Pan H, Xu W, Wang Y. Dyeing and characterization of cellulose powder developed from waste cotton. Polymers (Basel). 2019;11(12):1982. Aluigi A, Sotgiu G, Torreggiani A, Guerrini A, Orlandi VT, Corticelli F, Varchi G. Methylene Blue doped films of wool keratin with antimicrobial photodynamic activity. ACS Appl Mater Interfaces. 2015;7(31):17416–24.Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. (1998). "Proteins: Three-Dimensional Structure" (PDF). Fundamentals of Biochemistry. Wiley. p.158. ISBN 978-0-471-58650-0. Archived (PDF) from the original on 2006-09-17. Fibrous proteins are characterized by a single type of secondary structure: a keratin is a left-handed coil of two a helices