Long-term stability of protein secondary structure in dry seeds

Comparative Biochemistry and Physiology - A Physiology

Volumn 117, Issue 3, 1997, Pages 343-348

  Golovina, Elena A ^a,b   Wolkers, Willem F ^a   Hoekstra, Folkert A ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b TIMIRYAZEV INSTITUTE OF PLANT PHYSIOLOGY   (Russian Federation)

Author keywords

desiccation tolerance; FTIR spectroscopy; glassy state; protein denaturation; protein secondary structure; protein protein interaction; seed; seed aging

Indexed keywords

CONFERENCE PAPER; FOURIER ANALYSIS; NONHUMAN; PLANT SEED; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

EID: 0031195268     PISSN: 03009629     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9629(96)00273-3     Document Type: Conference Paper

References (32)

1. Barton L.V. Seed Preservation and Longevity. 1961;Interscience Publishers, New York.
2. Bewley J.D., Black M. Seeds, Physiology of Development and Germination. 1994;Plenum Press, New York. 1-445.
3. 13C=O-labeled phospholipids hydrogen bonding to carbonyl groups. Biochemistry. 27:1988;8239-8249.
4. Brown J.W.S., Ersland D.R., Hall T.C. Molecular aspects of storage protein synthesis during seed development. Khan A.A. The Physiology of Seed Development, Dormancy and Germination. 1982;3-42 Elsevier Biomedical Press, New York.
5. Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 25:1986;469-487.
6. Carpenter J.F., Crowe J.H. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry. 28:1989;3916-3922.
7. Crocker W., Groves J.F. A method of prophesying the life duration of seeds. Proc. Natl. Acad. Sci. USA. 1:1915;152-155.
8. Crowe J.H., Crowe L.M., Carpenter J.F., Aurell Wistrom C. Stabilization of dry phospholipid bilayers and proteins by sugars. Biochem. J. 242:1987;1-10.
9. Crowe J.H., Crowe L.M., Chapman D. Preservation of membranes in anhydrobiotic organisms. the role of trehalose Science. 223:1984;701-703.
10. Crowe J.H., Hoekstra F.A., Crowe L.M. Anhydrobiosis. Annu. Rev. Physiol. 54:1992;570-599.
11. Ellis R.H., Roberts E.H. The influence of temperature and moisture on seed viability period in barley (Hordeum distichum L.). Ann. Bot. 45:1980;31-37.
12. Hoekstra F.A. Collecting pollen for genetic resources conservation. Guarino L., Ramanatha Rao V., Reid R. Collecting Plant Genetic Diversity. 1995;527-550 CAB International, Oxon, UK.
13. Hoekstra F.A., Wolkers W.F., Buitink J., Golovina E.A., Crowe J.H., Crowe L.M. Membrane stabilization in the dry state. Comp. Biochem. Physiol. 117A:1997;335-341.
14. Holloway P.W., Mantsch H.H. Structure of Cytochrome b5 in solution by Fourier-transform infrared spectroscopy. Biochemistry. 28:1989;931-935.
15. Koster K.L. Glass formation and desiccation tolerance in seeds. Plant Physiol. 96:1991;302-304.
16. Mantsch H.H., Perczel A., Hollosi M., Fasman G.D. Characterization of β-turns in cyclic hexapeptides in solution by Fourier transform IR spectroscopy. Biopolymers. 33:1993;201-207.
17. Niethammer A., Tietz N. Samen und Früchte des Handels und der Industrie:1961;Dr. W. Junk Uitgeverij, 's-Gravenhage, The Netherlands. 180-183.
18. Prestrelski S.J., Tedeschi N., Arakawa T., Carpenter J.F. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 65:1993;661-671.
19. Priestley D.A. Seed Aging. implications for Seed Storage and Persistence in Soil:1986;Comstock Publ. Assoc, Ithaca and London. 1-304.
20. Priestley D.A., Posthumus M.A. Extreme longevity of lotus seeds from Pulantien. Nature. 211:1982;148-149.
21. Sanders J.C., Haris P.I., Chapman D., Otto C., Hemminga M.A. Secondary structure of M13 coat protein in phospholipids studied by circular dichroism, Raman, and Fourier transform infrared spectroscopy. Biochemistry. 32:1993;12446-12454.
22. Sarver R.W., Krueger W.C. Infrared investigation on the conformation of proteins deposited on polyethylene films. Anal. Biochem. 212:1993;519-525.
23. Shen-Miller J., Schopf J.W., Beyer R. Germination of a ca. 700-year-old lotus seed from China. evidence of exceptional longevity of seed viability Am. J. Bot. 70:1982;78.
24. Surewicz W.K., Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta. 952:1988;115-130.
25. Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy. a critical assessment Biochemistry. 32:1993;389-394.
26. 2O solutions. J. Biol. Chem. 242:1967;5460-5466.
27. Susi H. Structure and stability of biological macromolecules. Biological Macromolecules, Vol. 2. 1969;525-663 Marcel Dekker, New York.
28. van Bilsen D.G.J.L., Hoekstra F.A. Decreased membrane integrity in aging Typha latifolia L. pollen. accumulation of lysolipids and free fatty acids Plant. Physiol. 101:1993;675-682.
29. van Bilsen D.G.J.L., Hoekstra F.A., Crowe L.M., Crowe J.H. Altered phase behavior in membranes of aging dry pollen may cause imbibitional leakage. Plant. Physiol. 104:1994;1193-1199.
30. Williams R.J., Leopold A.C. The glassy state in corn embryos. Plant Physiol. 89:1989;977-981.
31. Wolkers W.F., Hoekstra F.A. Aging of dry desiccation tolerant pollen does not affect protein secondary structure. Plant Physiol. 109:1995;907-915.
32. Wolkers W.F., Hoekstra F.A. Heat stability in desiccation tolerant cattail pollen (Typha latifolia). A Fourier transform infrared study. Comp. Biochem. Physiol. 117A:1997;349-355.