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Digitale Medien

Investigation of differences in the tertiary structures of food proteins by small-angle X-ray scattering (1988)

Pessen, Helmut ; Kumosinski, Thomas F. ; Farrell, Harold M.

Springer

Journal of industrial microbiology and biotechnology 3 (1988), S. 89-103

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ISSN: 1476-5535

Schlagwort(e): Food protein ; Milk protein ; Egg protein ; Protein structure, tertiary ; Small-angle scattering ; β-Lactoglobulin ; α-Lactalbumin ; Lysozyme ; Ribonuclease ; Riboflavin-binding protein

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: Summary With current emphasis in bioengineering on developing new and better structure-function relationships for proteins (e.g., the need for predictability of expected properties prior to cloning), practical and reliable methodology for providing characterization of appropriate features has become of increasing importance. The most potent and detailed technique, X-ray crystallography, has severe limitations: it is so demanding and time-consuming that X-ray coordinates are frequently unavailable for materials of interest; its data relate to static and essentially unhydrated structures, whereas proteins exhibit a variety of dynamic features and function in an aqueous environment; and many proteins of technological importance may never be crystallized. Small-angle X-ray scattering, however, is particularly suitable as a methodology that can provide a substantial number of significant geometric parameters consistent with crystallographic results, that can readily show tertiary structural changes occurring under varying conditions, and that can deal with solutions and gels. Results are presented here from small-angle X-ray scattering investigations of the apo and holo forms of chicken egg-white riboflavin-binding protein, chicken egg-white lysozyme, bovine milk-whey α-lactalbumin and β-lactoglobulin, and bovine ribonuclease. We utilize these observations to compare tertiary structures of these proteins as well as conformational changes in these structures, and to provide a basis for discussion of their physical and biological significance.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01569550

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Digitale Medien

Influence of Neutral Salts on the Hydrothermal Stability of Acid-Soluble Collagen (2000)

Brown, Eleanor M. ; Farrell, Harold M. ; Wildermuth, Renee J.

Springer

The protein journal 19 (2000), S. 85-92

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ISSN: 1573-4943

Schlagwort(e): Soluble collagen ; thermal stability ; NaCl ; KCl

Quelle: Springer Online Journal Archives 1860-2000

Thema: Chemie und Pharmazie

Notizen: Abstract The thermal stability of acid-soluble collagens was studied by circular dichroism (CD) spectroscopy. Adult bovine dermal collagen (BDC), rat-tail tendon collagen (RTC), and calf skin collagen (CSC) were compared. Despite some variability in amino acid composition and apparent molecular weight, the CD spectra for helical and unordered collagen structures were essentially the same for all the sources. The melting of these collagens occurs as a two-stage process characterized by a pretransition (T p) followed by complete denaturation (T d). The characteristic temperatures vary with the source of the collagen; for mature collagens (BDC, RTC) T p = 30°C and T d = 36deg;C, and for CSC T p = 34°C and T d = 40°C. Neutral salts, NaCl or KCl, at low concentrations (0.02–0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1023/A:1007074314686

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