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The Conformation of a Soluble Wool Keratin Derivative

BS Harrap
16(1) pp.231 - 240


39 articles found in Crossref database.

A study of a low‐sulphur wool keratin derivative in formamide‐water mixtures
DeDeurwaerder R., Harrap B. S.
Die Makromolekulare Chemie. 1964 72(1). p.1
Low‐sulfur proteins from α‐keratins. Interrelationships between their amino acid compositions, α‐helix contents, and the supercontraction of the parent keratin
Crewther W. G., Gillespie J. M., Harrap B. S., Inglis A. S.
Biopolymers. 1966 4(8). p.905
Thermal Transitions in Keratin
Mason P.
Textile Research Journal. 1965 35(6). p.483
The Preparation and Properties of a Helix-rich Fraction Obtained by Partial Proteolysis of Low Sulfur S-Carboxymethylkerateine from Wool
Crewther W.G., Harrap B.S.
Journal of Biological Chemistry. 1967 242(19). p.4310
Proton magnetic resonance study of conformational transitions in heterogeneous oxidized-wool proteins
Dale B.J., Jones D.W.
Polymer. 1973 14(10). p.523
A note on the role of the microfibrils in the mechanical properties of α-keratins
Feughelman M.
Journal of Macromolecular Science, Part B. 1979 16(1). p.155
Isolierung und Untersuchung von löslichen Wollproteinbestandteilen aus hydrolytisch geschädigter Wolle (1975)
Baumann Hanno
Conformational studies of the α-helical proteins from wool keratin by c.d.
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International Journal of Biological Macromolecules. 1982 4(3). p.165
The viscoelasticity and structure of keratin and collagen
Mason P.
Kolloid-Zeitschrift & Zeitschrift für Polymere. 1965 202(2). p.139
Cooperative unfolding of α‐keratin
Feughelman M.
Journal of Applied Polymer Science. 1966 10(12). p.1937
Aggregation of wool keratin intermediate filament proteins
Woods E.F.
International Journal of Biological Macromolecules. 1989 11(5). p.278
Studies of an associating protein system: Sub‐unit molecular weight of the low sulphur fraction of soluble wool keratin
Dedeurwaerder R., Harrap B. S.
Die Makromolekulare Chemie. 1965 86(1). p.98
The Longitudinal Mechanical Properties of Wool Fibers and Their Relationship to The Low Sulfur Keratin Fraction
Feughelman M., Reis P.J.
Textile Research Journal. 1967 37(4). p.334
β‐Chain conformation of the high‐sulfur proteins from wool
Amiya Takayuki, Miyamoto Takeaki, Inagaki Hiroshi
Biopolymers. 1980 19(5). p.1093
Selective Cross-Linking in the Micronbrillar Component of Keratin
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Textile Research Journal. 1968 38(6). p.674
12—THE FORMATION OF LYSINOALANINE AND LANTHIONLNE IN WOOL FIBRES STRETCHED IN BOILING WATER, AND THEIR RELATION TO PERMANENT SET
Robson A., Williams M. J., Woodhouse J. M.
Journal of the Textile Institute. 1969 60(4). p.140
The Primary Structure of a Protein, Component 0.62, Rich in Glycine and Aromatic Residues, Obtained from Wool Keratin
Dopheide Theo A. A.
European Journal of Biochemistry. 1973 34(1). p.120
Thermal transitions of synthetic and biological polymers in bulk and in solution
Mason P., Rigby B.J.
Polymer. 1965 6(2). p.90
The Proteins Composition, Structure, and Function (1966)
SEIFTER SAM, GALLOP PAUL M.
Biology of the Integument (1986)
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Bestimmung von Aminosäuresequenzen in α-Keratose
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Kolloid-Zeitschrift & Zeitschrift für Polymere. 1967 220(2). p.107
The Stress—Strain Characteristics of Animal Fibers After Reduction and Alkylation
Crewther W.G.
Textile Research Journal. 1965 35(10). p.867
Investigations into charge heterogeneity of wool intermediate filament proteins
Paton Louise N., Gerrard Juliet A., Bryson Warren G.
Journal of Proteomics. 2008 71(5). p.513
Thermal denaturation and structural changes of α-helical proteins in keratins
Wortmann Franz J., Wortmann Gabriele, Marsh Jennifer, Meinert Knut
Journal of Structural Biology. 2012 177(2). p.553
The Effects of Disaggregating Agents on the Stress-Strain Relationship for Wool Fibers
Crewter W.G.
Textile Research Journal. 1972 42(2). p.77
Hair and Hair Diseases (1990)
Baden H. P.
THE CONFORMATION OF THE HIGH‐SULPHUR PROTEINS OF WOOL. I. THE PREPARATION AND PROPERTIES OF A WATER‐SOLUBLE METAKERATIN
Bhatnagar G. M., Crewther W. G.
International Journal of Protein Research. 1969 1(1-4). p.199
A high-resolution solid-state 13C NMR study on conformation and molecular motion of low-sulfur keratin protein films obtained from wool
Yoshimizu Hiroaki, Mimura Hiroyuki, Ando Isao
Journal of Molecular Structure. 1991 246(3-4). p.367
(1973)
Bradbury J.H.
The Effect of Formaldehyde on Wool Before, During and After Contraction in Lithium Bromide Solution
Griffith June C., Mason P.
Textile Research Journal. 1966 36(11). p.1021
Reversibility of thermal transitions in proteins: Racemization and aggregation as factors in the reversible denaturation of a soluble keratin derivative (SCMKA)
Harrap B. S.
Biopolymers. 1969 8(2). p.187
Rapid and Specific Effects of Bromine on the System Keratin/Formic Acid
GRIFFITH JUNE C., MASON P.
Nature. 1966 211(5056). p.1399
Advances in Protein Chemistry Volume 20 (1965)
Crewther W.G., Fraser R.D.B., Lennox F.G., Lindley H.
Structure of α-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments
Parry D.A.D., Crewther W.G., Fraser R.D.B., MacRae T.P.
Journal of Molecular Biology. 1977 113(2). p.449
28—EXAMINATION IN THE ELECTRON MICROSCOPE OFS-CARBOXYMETHYLKERATEINE-A AND OF THE HELIX-RICH FRACTION OBTAINED FROM IT BY PARTIAL PROTEOLYSIS
Dobb M. G., Millward G. R., Crewther W. G.
The Journal of The Textile Institute. 1973 64(6). p.374
Helix-rich Fraction from the Low-sulphur Proteins of Wool
CREWTHER W. G., HARRAP B. S.
Nature. 1965 207(4994). p.295
Thermal transitions in reduced wool fibers
Frazer L. A., Leach S. J., Milligan B.
Journal of Applied Polymer Science. 1968 12(8). p.1992
Effect of Formic Acid on the Structure of α-Keratin
BENDIT E. G.
Nature. 1966 211(5055). p.1257
Chemistry of Natural Protein Fibers (1977)
Lindley H.
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