메뉴 건너뛰기




Volumn 277, Issue C, 2009, Pages 137-156

Chapter 4 Cytomechanics of Hair. Basics of the Mechanical Stability

Author keywords

Keratin; Cortex; Cuticle; Hair; Intermediate filament; Stress strain behavior; Water swelling

Indexed keywords

ALPHA KERATIN; ARGININE; CYSTEIC ACID; CYSTINE; DISULFIDE; HYDROGEN; ISOLEUCINE; KERATIN; LEUCINE; MELANIN; METHIONINE; PHENYLALANINE; PROLINE; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; WATER;

EID: 74949101530     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(09)77004-2     Document Type: Review
Times cited : (26)

References (72)
  • 1
    • 0002583785 scopus 로고
    • X-ray studies of the structure of hair, wool, and related fibres. I General
    • Astbury W.T., and Street A. X-ray studies of the structure of hair, wool, and related fibres. I General. Phil. Trans. Roy. Soc. A 230 (1931) 75-101
    • (1931) Phil. Trans. Roy. Soc. A , vol.230 , pp. 75-101
    • Astbury, W.T.1    Street, A.2
  • 4
    • 10444263886 scopus 로고
    • Torsional properties of hair in relation to permanent waving and setting
    • Bogaty H. Torsional properties of hair in relation to permanent waving and setting. J. Soc. Cosmet. Chem. 18 (1967) 575-580
    • (1967) J. Soc. Cosmet. Chem. , vol.18 , pp. 575-580
    • Bogaty, H.1
  • 5
    • 11144324103 scopus 로고
    • Separation of chemically unmodified histological components of keratin fibres and analyses of cuticles
    • Bradbury J.H., Chapman G.V., Hambly A.N., and King N.L.R. Separation of chemically unmodified histological components of keratin fibres and analyses of cuticles. Nature 210 (1966) 1333-1334
    • (1966) Nature , vol.210 , pp. 1333-1334
    • Bradbury, J.H.1    Chapman, G.V.2    Hambly, A.N.3    King, N.L.R.4
  • 6
    • 0030636238 scopus 로고    scopus 로고
    • Hair melanin and hair color
    • Jolles P., Zahn H., and Höcker H. (Eds), Birkhauser Verlag, Basel
    • Castanet J., and Ortonne J.-P. Hair melanin and hair color. In: Jolles P., Zahn H., and Höcker H. (Eds). Formation and Structure of Human Hair (1997), Birkhauser Verlag, Basel 209-226
    • (1997) Formation and Structure of Human Hair , pp. 209-226
    • Castanet, J.1    Ortonne, J.-P.2
  • 7
    • 84964153039 scopus 로고
    • A mechanical model for wool and other keratin fibers
    • Chapman B.M. A mechanical model for wool and other keratin fibers. Text. Res. J. 39 (1969) 1102-1109
    • (1969) Text. Res. J. , vol.39 , pp. 1102-1109
    • Chapman, B.M.1
  • 8
    • 77951628380 scopus 로고
    • On polymeric materials containing fibrils with a phase transition. Part III. The effect of slip at the fibril matrix interface
    • Chapman B.M., and Hearle J.W.S. On polymeric materials containing fibrils with a phase transition. Part III. The effect of slip at the fibril matrix interface. J. Macromol. Sci. Phys. B 4 (1970) 127-151
    • (1970) J. Macromol. Sci. Phys. B , vol.4 , pp. 127-151
    • Chapman, B.M.1    Hearle, J.W.S.2
  • 9
    • 84965853424 scopus 로고
    • The stress-strain characteristics of animal fibers after reduction and alkylation
    • Crewther W.G. The stress-strain characteristics of animal fibers after reduction and alkylation. Text. Res. J. 35 (1956) 867-877
    • (1956) Text. Res. J. , vol.35 , pp. 867-877
    • Crewther, W.G.1
  • 11
    • 34250468665 scopus 로고
    • Mechanical properties of keratin fibres between - 196 °C and 20 °C
    • Druhala M., and Feughelman M. Mechanical properties of keratin fibres between - 196 °C and 20 °C. Kolloid. ZZ Polym. 248 (1971) 1032-1033
    • (1971) Kolloid. ZZ Polym. , vol.248 , pp. 1032-1033
    • Druhala, M.1    Feughelman, M.2
  • 12
    • 0016061738 scopus 로고
    • Dynamic mechanical loss in keratin at low temperatures
    • Druhala M., and Feughelman M. Dynamic mechanical loss in keratin at low temperatures. Colloid. Polym. Sci. 252 (1974) 381-391
    • (1974) Colloid. Polym. Sci. , vol.252 , pp. 381-391
    • Druhala, M.1    Feughelman, M.2
  • 13
    • 33644993766 scopus 로고    scopus 로고
    • In vivo formation steps of the hard α-keratin intermediate filament along a hair follicle: evidence for structural poly-morphism
    • Er Rafik M., Briki F., Burghammer M., and Doucet J. In vivo formation steps of the hard α-keratin intermediate filament along a hair follicle: evidence for structural poly-morphism. J. Struct. Biol. 154 (2006) 79-88
    • (2006) J. Struct. Biol. , vol.154 , pp. 79-88
    • Er Rafik, M.1    Briki, F.2    Burghammer, M.3    Doucet, J.4
  • 14
    • 84964165967 scopus 로고
    • A two-phase structure for keratin fibers
    • Feughelman M. A two-phase structure for keratin fibers. Text. Res. J. 29 (1959) 223-228
    • (1959) Text. Res. J. , vol.29 , pp. 223-228
    • Feughelman, M.1
  • 15
    • 0000036273 scopus 로고
    • A note on the role of the microfibrils in the mechanical properties of α-keratins
    • Feughelman M. A note on the role of the microfibrils in the mechanical properties of α-keratins. J. Macromol. Sci. Phys. B 16 (1979) 155-162
    • (1979) J. Macromol. Sci. Phys. B , vol.16 , pp. 155-162
    • Feughelman, M.1
  • 16
    • 0001442128 scopus 로고
    • The mechanical properties of wool keratin and its molecular configuration
    • Feughelman M., and Hally A.R. The mechanical properties of wool keratin and its molecular configuration. Kolloid Z. 168 (1960) 107-115
    • (1960) Kolloid Z. , vol.168 , pp. 107-115
    • Feughelman, M.1    Hally, A.R.2
  • 17
    • 0028410921 scopus 로고
    • A model for the mechanical properties of the α-keratin cortex
    • Feughelman M. A model for the mechanical properties of the α-keratin cortex. Text. Res. J. 64 (1994) 236-239
    • (1994) Text. Res. J. , vol.64 , pp. 236-239
    • Feughelman, M.1
  • 19
    • 0019063552 scopus 로고
    • Degradation of protein disulphide bonds in dilute alkali
    • Florence T.M. Degradation of protein disulphide bonds in dilute alkali. Biochem. J. 189 (1980) 507-520
    • (1980) Biochem. J. , vol.189 , pp. 507-520
    • Florence, T.M.1
  • 20
    • 0000426664 scopus 로고
    • Influence of diluent and of copolymer composition on the glass temperature of a polymer system
    • Fox T.G. Influence of diluent and of copolymer composition on the glass temperature of a polymer system. Bull. Am. Phys. Soc. 1 (1956) 123
    • (1956) Bull. Am. Phys. Soc. , vol.1 , pp. 123
    • Fox, T.G.1
  • 21
    • 0019300768 scopus 로고
    • Molecular structure and mechanical properties of keratins
    • Fraser R.D.B., and MacRae T.P. Molecular structure and mechanical properties of keratins. Symp. Soc. Exp. Biol. 34 (1980) 211-246
    • (1980) Symp. Soc. Exp. Biol. , vol.34 , pp. 211-246
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 22
    • 12444334727 scopus 로고
    • The fine structure of keratin fibres
    • Breuer M.M. (Ed), American Chemical Society, USA
    • Fraser R.D.B., and MacRae T.P. The fine structure of keratin fibres. In: Breuer M.M. (Ed). Milton Harris: Chemist, Innovator and Entrepreneur (1982), American Chemical Society, USA 119-137
    • (1982) Milton Harris: Chemist, Innovator and Entrepreneur , pp. 119-137
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 23
    • 0037403823 scopus 로고    scopus 로고
    • Macrofibril assembly in trichocyte (hard α-) keratins
    • Fraser R.D.B., and Parry D.A.D. Macrofibril assembly in trichocyte (hard α-) keratins. J. Struct. Biol. 142 (2003) 319-325
    • (2003) J. Struct. Biol. , vol.142 , pp. 319-325
    • Fraser, R.D.B.1    Parry, D.A.D.2
  • 25
    • 0027466836 scopus 로고
    • Sequence, expression, and evolutionary conservation of a gene encoding a glycine/tyrosine-rich keratin-associated protein of hair
    • Fratini A., Powell B.C., and Rogers G.E. Sequence, expression, and evolutionary conservation of a gene encoding a glycine/tyrosine-rich keratin-associated protein of hair. J. Biol. Chem. 268 (1993) 4511-4518
    • (1993) J. Biol. Chem. , vol.268 , pp. 4511-4518
    • Fratini, A.1    Powell, B.C.2    Rogers, G.E.3
  • 26
    • 0342362498 scopus 로고
    • The structural mechanics of fibers
    • Hearle J.W.S. The structural mechanics of fibers. J. Polym. Sci. C 20 (1967) 215-251
    • (1967) J. Polym. Sci. C , vol.20 , pp. 215-251
    • Hearle, J.W.S.1
  • 27
    • 0008652938 scopus 로고
    • The Chapman mechanical model for wool and other keratin fibres
    • Hearle J.W.S. The Chapman mechanical model for wool and other keratin fibres. Text. Res. J. 39 (1969) 1109
    • (1969) Text. Res. J. , vol.39 , pp. 1109
    • Hearle, J.W.S.1
  • 28
    • 0034029857 scopus 로고    scopus 로고
    • A critical review of the structural mechanics of wool and hair fibres
    • Hearle J.W.S. A critical review of the structural mechanics of wool and hair fibres. Int. J. Biol. Macromol. 27 (2000) 123-138
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 123-138
    • Hearle, J.W.S.1
  • 29
    • 0038353879 scopus 로고    scopus 로고
    • A total model for the structural mechanics of wool
    • Hearle J.W.S. A total model for the structural mechanics of wool. Wool Tech. Sheep Breed 5 (2003) 95-117
    • (2003) Wool Tech. Sheep Breed , vol.5 , pp. 95-117
    • Hearle, J.W.S.1
  • 30
    • 0343667664 scopus 로고
    • On polymeric materials containing fibrils with a phase transition I. General discussion of mechanics applied particularly to wool fibers
    • Hearle J.W.S., and Chapman B.M. On polymeric materials containing fibrils with a phase transition I. General discussion of mechanics applied particularly to wool fibers. J. Macromol. Sci. Phys. B 2 (1968) 663-695
    • (1968) J. Macromol. Sci. Phys. B , vol.2 , pp. 663-695
    • Hearle, J.W.S.1    Chapman, B.M.2
  • 31
    • 84945779683 scopus 로고
    • On polymeric materials containing fibrils with a phase transition. II. The mechanical consequences of matrix shear
    • Hearle J.W.S., and Chapman B.M. On polymeric materials containing fibrils with a phase transition. II. The mechanical consequences of matrix shear. J. Macromol. Sci. Phys. B 2 (1968) 697-741
    • (1968) J. Macromol. Sci. Phys. B , vol.2 , pp. 697-741
    • Hearle, J.W.S.1    Chapman, B.M.2
  • 33
    • 0004904228 scopus 로고
    • Investigations of the cell membrane complex and its modifications during industrial processing of wool
    • Herrling J., and Zahn H. Investigations of the cell membrane complex and its modifications during industrial processing of wool. Proc. 7th Int. Wool Text. Res. Conf., Tokio 1 (1985) 181-193
    • (1985) Proc. 7th Int. Wool Text. Res. Conf., Tokio , vol.1 , pp. 181-193
    • Herrling, J.1    Zahn, H.2
  • 34
    • 0026360598 scopus 로고
    • DSC investigation of the physical ageing and deageing of wool
    • Huson M.G. DSC investigation of the physical ageing and deageing of wool. Polym. Int. 26 (1991) 157-161
    • (1991) Polym. Int. , vol.26 , pp. 157-161
    • Huson, M.G.1
  • 35
    • 70049106938 scopus 로고    scopus 로고
    • Nonisothermal kinetics of hard α-keratin thermal denaturation
    • doi:10.1002/mabi.200800344
    • Istrate D., Popescu C., and Möller M. Nonisothermal kinetics of hard α-keratin thermal denaturation. Macromol. Biosci. (2009) doi:10.1002/mabi.200800344
    • (2009) Macromol. Biosci.
    • Istrate, D.1    Popescu, C.2    Möller, M.3
  • 37
    • 0027987929 scopus 로고
    • Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis P.D., Hutton E., and Fuchs E. Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. J. Cell Biol. 127 (1994) 1049-1060
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 38
    • 0030852146 scopus 로고    scopus 로고
    • The glass transition of wool: an improved determination using DSC
    • Kure J.M., Pierlot A.P., Russell I.M., and Shanks R.A. The glass transition of wool: an improved determination using DSC. Text. Res. J. 67 (1997) 18-22
    • (1997) Text. Res. J. , vol.67 , pp. 18-22
    • Kure, J.M.1    Pierlot, A.P.2    Russell, I.M.3    Shanks, R.A.4
  • 39
    • 0008163543 scopus 로고
    • H-bond dissociation in hydrogen bond dominated solids
    • Nissan A.H. H-bond dissociation in hydrogen bond dominated solids. Macromolecules 9 (1976) 840-850
    • (1976) Macromolecules , vol.9 , pp. 840-850
    • Nissan, A.H.1
  • 40
    • 34248197448 scopus 로고    scopus 로고
    • Nanomechanics of single keratin fibres: a Raman study of the α-helix→β-sheet transition and the effect of water
    • Paquin R., and Colomban P. Nanomechanics of single keratin fibres: a Raman study of the α-helix→β-sheet transition and the effect of water. J. Raman Spectrosc. 38 (2007) 504-514
    • (2007) J. Raman Spectrosc. , vol.38 , pp. 504-514
    • Paquin, R.1    Colomban, P.2
  • 41
    • 0028983054 scopus 로고
    • Hard-keratin IF: a structural model lacking a head-to-tail molecular overlap but having hybrid features characteristic of both epidermal keratin and vimentin IF
    • Parry D.A.D. Hard-keratin IF: a structural model lacking a head-to-tail molecular overlap but having hybrid features characteristic of both epidermal keratin and vimentin IF. Proteins 22 (1995) 267-272
    • (1995) Proteins , vol.22 , pp. 267-272
    • Parry, D.A.D.1
  • 42
    • 0029902659 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filaments: an alternative interpretation of the low-angle equatorial X-ray diffraction pattern and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks
    • Parry D.A.D. Hard α-keratin intermediate filaments: an alternative interpretation of the low-angle equatorial X-ray diffraction pattern and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks. Int. J. Biol. Macromol. 19 (1996) 45-50
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 45-50
    • Parry, D.A.D.1
  • 43
    • 17444414616 scopus 로고    scopus 로고
    • Microdissection of the sequence and structure of intermediate filament chains
    • Parry D.A.D. Microdissection of the sequence and structure of intermediate filament chains. Adv. Protein Chem. 70 (2005) 113-142
    • (2005) Adv. Protein Chem. , vol.70 , pp. 113-142
    • Parry, D.A.D.1
  • 44
    • 0001292056 scopus 로고
    • Intermediate filament structure. 1. Analysis of IF protein sequence data
    • Parry D.A.D., and Fraser R.D.B. Intermediate filament structure. 1. Analysis of IF protein sequence data. Int. J. Biol. Macromol. 7 (1985) 203-213
    • (1985) Int. J. Biol. Macromol. , vol.7 , pp. 203-213
    • Parry, D.A.D.1    Fraser, R.D.B.2
  • 45
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism
    • Parry D.A.D., and Steinert P.M. Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism. Q. Rev. Biophys. 32 (1999) 99-187
    • (1999) Q. Rev. Biophys. , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 46
    • 0022024708 scopus 로고
    • Detecting a glass transition in wool by differential scanning calorimetry
    • Phillips D.G. Detecting a glass transition in wool by differential scanning calorimetry. Text. Res. J. 55 (1985) 171-174
    • (1985) Text. Res. J. , vol.55 , pp. 171-174
    • Phillips, D.G.1
  • 47
    • 34547240716 scopus 로고    scopus 로고
    • Hair-the most sophisticated biological composite material
    • Popescu C., and Höcker H. Hair-the most sophisticated biological composite material. Chem. Soc. Rev. 36 (2007) 1282-1291
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1282-1291
    • Popescu, C.1    Höcker, H.2
  • 48
    • 0030636267 scopus 로고    scopus 로고
    • The role of keratin proteins and their genes in the growth, structure and properties of hair
    • Jolles P., Zahn H., and Höcker H. (Eds), Birkhauser Verlag, Basel
    • Powell B.C., and Rogers G.E. The role of keratin proteins and their genes in the growth, structure and properties of hair. In: Jolles P., Zahn H., and Höcker H. (Eds). Formation and Structure of Human Hair (1997), Birkhauser Verlag, Basel 59-149
    • (1997) Formation and Structure of Human Hair , pp. 59-149
    • Powell, B.C.1    Rogers, G.E.2
  • 50
    • 0001284036 scopus 로고
    • The reactivity of the sulphur linkage in animal fibres-Part I. The chemical mechanism of permanent set
    • Speakman J.B. The reactivity of the sulphur linkage in animal fibres-Part I. The chemical mechanism of permanent set. J. Soc. Dyers Colourists 52 (1936) 335-341
    • (1936) J. Soc. Dyers Colourists , vol.52 , pp. 335-341
    • Speakman, J.B.1
  • 51
    • 2142740135 scopus 로고
    • Small-angle X-ray scattering investigations of the matrix in α-keratin (in German)
    • Spei M. Small-angle X-ray scattering investigations of the matrix in α-keratin (in German). Kolloid Z.u.Z, Polymere 250 (1972) 214-221
    • (1972) Kolloid Z.u.Z, Polymere , vol.250 , pp. 214-221
    • Spei, M.1
  • 52
    • 84965372000 scopus 로고
    • Structure of α-keratin
    • Spei M. Structure of α-keratin. Text. Res. J. 43 (1973) 692-693
    • (1973) Text. Res. J. , vol.43 , pp. 692-693
    • Spei, M.1
  • 53
    • 34250445606 scopus 로고
    • Small-angle X-ray scattering of the stretched keratin fibre (in German)
    • Spei M., and Zahn H. Small-angle X-ray scattering of the stretched keratin fibre (in German). Monatsh. Chem. 102 (1971) 1163
    • (1971) Monatsh. Chem. , vol.102 , pp. 1163
    • Spei, M.1    Zahn, H.2
  • 54
    • 16544363159 scopus 로고
    • The influence of anionic tensides on the XRD spectrum of fibrous keratins (in German)
    • Spei M., Stein W., and Zahn H. The influence of anionic tensides on the XRD spectrum of fibrous keratins (in German). Kolloid Z.u.Z. Polymere 238 (1970) 447-454
    • (1970) Kolloid Z.u.Z. Polymere , vol.238 , pp. 447-454
    • Spei, M.1    Stein, W.2    Zahn, H.3
  • 55
    • 0001295175 scopus 로고
    • Molecular and cellular biology of keratins
    • Goldsmith L.A. (Ed), Oxford University Press, New York
    • Steinert P.M., and Freedberg I.M. Molecular and cellular biology of keratins. In: Goldsmith L.A. (Ed). Physiology, Biochemistry, and Molecular Biology of the Skin vol. I (1991), Oxford University Press, New York 113-147
    • (1991) Physiology, Biochemistry, and Molecular Biology of the Skin , vol.I , pp. 113-147
    • Steinert, P.M.1    Freedberg, I.M.2
  • 57
    • 0029589997 scopus 로고
    • Some simple theoretical considerations on the bending stiffness of human hair
    • Swift J.A. Some simple theoretical considerations on the bending stiffness of human hair. Int. J. Cosmetic Sci. 17 (1995) 245-253
    • (1995) Int. J. Cosmetic Sci. , vol.17 , pp. 245-253
    • Swift, J.A.1
  • 58
    • 0002273821 scopus 로고    scopus 로고
    • Morphology and histochemistry of human hair
    • Jolles P., Zahn H., and Höcker H. (Eds), Birkhauser Verlag, Basel
    • Swift J.A. Morphology and histochemistry of human hair. In: Jolles P., Zahn H., and Höcker H. (Eds). Formation and Structure of Human hair (1997), Birkhauser Verlag, Basel 149-176
    • (1997) Formation and Structure of Human hair , pp. 149-176
    • Swift, J.A.1
  • 60
    • 84965911485 scopus 로고
    • Degradation of human hair by papain. Part III. Some electron microscope observations
    • Swift J.A., and Holmes A.W. Degradation of human hair by papain. Part III. Some electron microscope observations. Text. Res. J. 35 (1965) 1014-1019
    • (1965) Text. Res. J. , vol.35 , pp. 1014-1019
    • Swift, J.A.1    Holmes, A.W.2
  • 61
    • 0035696065 scopus 로고    scopus 로고
    • Microscopical investigations on the epicuticle of mammalian keratin fibres
    • Swift J.A., and Smith J.R. Microscopical investigations on the epicuticle of mammalian keratin fibres. J. Microscopy 204 (2001) 203-211
    • (2001) J. Microscopy , vol.204 , pp. 203-211
    • Swift, J.A.1    Smith, J.R.2
  • 62
    • 0034739847 scopus 로고    scopus 로고
    • In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding
    • Wang H., Parry D.A.D., Jones L.N., Idler W.W., Marekov L.N., and Steinert P.M. In vitro assembly and structure of trichocyte keratin intermediate filaments: a novel role for stabilization by disulfide bonding. J. Cell Biol. 151 (2000) 1459-1468
    • (2000) J. Cell Biol. , vol.151 , pp. 1459-1468
    • Wang, H.1    Parry, D.A.D.2    Jones, L.N.3    Idler, W.W.4    Marekov, L.N.5    Steinert, P.M.6
  • 63
    • 33646547262 scopus 로고    scopus 로고
    • Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
    • Wiita A.P., Ainavarapu S.R.K., Huang H.H., and Fernandez J.M. Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques. PNAS 103 (2006) 7222-7227
    • (2006) PNAS , vol.103 , pp. 7222-7227
    • Wiita, A.P.1    Ainavarapu, S.R.K.2    Huang, H.H.3    Fernandez, J.M.4
  • 65
    • 0027953051 scopus 로고
    • The stress/strain curve of α-keratin fibers and the structure of the intermediate filament
    • Wortmann F.-J., and Zahn H. The stress/strain curve of α-keratin fibers and the structure of the intermediate filament. Text. Res. J. 64 (1994) 737-743
    • (1994) Text. Res. J. , vol.64 , pp. 737-743
    • Wortmann, F.-J.1    Zahn, H.2
  • 66
    • 0021202706 scopus 로고
    • Glass transition temperature of wool as a function of regain
    • Wortmann F.-J., Rigby B.J., and Phillips D.G. Glass transition temperature of wool as a function of regain. Text. Res. J. 54 (1984) 6-8
    • (1984) Text. Res. J. , vol.54 , pp. 6-8
    • Wortmann, F.-J.1    Rigby, B.J.2    Phillips, D.G.3
  • 67
    • 33645701083 scopus 로고    scopus 로고
    • The effect of water on the glass transition of human hair
    • Wortmann F.-J., Stapels M., Elliott R., and Chandra L. The effect of water on the glass transition of human hair. Biopolymers 81 (2006) 371-375
    • (2006) Biopolymers , vol.81 , pp. 371-375
    • Wortmann, F.-J.1    Stapels, M.2    Elliott, R.3    Chandra, L.4
  • 68
    • 84984306128 scopus 로고
    • The hair from the chemists' point of view (in German)
    • Zahn H. The hair from the chemists' point of view (in German). Chemie in unserer Zeit 23 (1989) 141-150
    • (1989) Chemie in unserer Zeit , vol.23 , pp. 141-150
    • Zahn, H.1
  • 69
    • 0026023755 scopus 로고
    • On the role of Mohair for the research of keratine (in German)
    • Zahn H. On the role of Mohair for the research of keratine (in German). Melliand-Textilber. 72 (1991) 926-931
    • (1991) Melliand-Textilber. , vol.72 , pp. 926-931
    • Zahn, H.1
  • 71
    • 71649089792 scopus 로고    scopus 로고
    • Wool from animal sources
    • Biopolymers. Steinbüchel A., and Fahnestock S.R. (Eds), Wiley-VCH Verlag GmbH & Co, Germany
    • Zahn H., Schaefer K., and Popescu C. Wool from animal sources. In: Steinbüchel A., and Fahnestock S.R. (Eds). Biopolymers. Polyamides and Complex Proteinaceous Materials II vol. 8 (2003), Wiley-VCH Verlag GmbH & Co, Germany 155-202
    • (2003) Polyamides and Complex Proteinaceous Materials II , vol.8 , pp. 155-202
    • Zahn, H.1    Schaefer, K.2    Popescu, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.