| Records |
| Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
| Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
Type |
Journal Article |
Year  |
1996 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
| Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
| Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
| Abstract |
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse. |
| Address |
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA |
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English |
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0027-8424 |
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| Notes |
PMID:8650166 |
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no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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| Author |
Hauser, M.D.; Kralik, J.; Botto-Mahan, C.; Garrett, M.; Oser, J. |
| Title |
Self-recognition in primates: phylogeny and the salience of species-typical features |
Type |
Journal Article |
| Year |
1995 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
| Volume |
92 |
Issue |
23 |
Pages |
10811-10814 |
| Keywords |
Animals; *Behavior, Animal; *Cognition; Discrimination (Psychology); Exploratory Behavior; Female; Hair Color; Male; Phylogeny; Psychology, Comparative; Research Design; Saguinus/*psychology; *Self Concept; Species Specificity; Touch; *Visual Perception |
| Abstract |
Self-recognition has been explored in nonlinguistic organisms by recording whether individuals touch a dye-marked area on visually inaccessible parts of their face while looking in a mirror or inspect parts of their body while using the mirror's reflection. Only chimpanzees, gorillas, orangutans, and humans over the age of approximately 2 years consistently evidence self-directed mirror-guided behavior without experimenter training. To evaluate the inferred phylogenetic gap between hominoids and other animals, a modified dye-mark test was conducted with cotton-top tamarins (Saguinus oedipus), a New World monkey species. The white hair on the tamarins' head was color-dyed, thereby significantly altering a visually distinctive species-typical feature. Only individuals with dyed hair and prior mirror exposure touched their head while looking in the mirror. They looked longer in the mirror than controls, and some individuals used the mirror to observe visually inaccessible body parts. Prior failures to pass the mirror test may have been due to methodological problems, rather than to phylogenetic differences in the capacity for self-recognition. Specifically, an individual's sensitivity to experimentally modified parts of its body may depend crucially on the relative saliency of the modified part (e.g., face versus hair). Moreover, and in contrast to previous claims, we suggest that the mirror test may not be sufficient for assessing the concept of self or mental state attribution in nonlinguistic organisms. |
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Department of Anthropology, Harvard University, Cambridge, MA 02138, USA |
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English |
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0027-8424 |
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PMID:7479889 |
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no |
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Equine Behaviour @ team @ |
Serial |
2825 |
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Hostikka, S.L.; Eddy, R.L.; Byers, M.G.; Hoyhtya, M.; Shows, T.B.; Tryggvason, K. |
| Title |
Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome |
Type |
Journal Article |
| Year |
1990 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
| Volume |
87 |
Issue |
4 |
Pages |
1606-1610 |
| Keywords |
Amino Acid Sequence; Base Sequence; Chromosome Mapping; Cloning, Molecular; Collagen/*genetics; Epitopes/analysis; Female; Fluorescent Antibody Technique; Gene Library; *Genes; Humans; Immunoblotting; Kidney/cytology/*metabolism; Macromolecular Substances; Molecular Sequence Data; Nephritis, Hereditary/*genetics; Oligopeptides/chemical synthesis/immunology; Placenta/metabolism; Pregnancy; Restriction Mapping; Sequence Homology, Nucleic Acid; *X Chromosome |
| Abstract |
We have identified and extensively characterized a type IV collagen alpha chain, referred to as alpha 5(IV). Four overlapping cDNA clones isolated contain an open reading frame for 543 amino acid residues of the carboxyl-terminal end of a collagenous domain, a 229-residue carboxyl-terminal noncollagenous domain, and 1201 base pairs coding for a 3' untranslated region. The collagenous Gly-Xaa-Yaa repeat sequence has five imperfections that coincide with those in the corresponding region of the alpha 1(IV) chain. The noncollagenous domain has 12 conserved cysteine residues and 83% and 63% sequence identity with the noncollagenous domains of the alpha 1(IV) and alpha 2(IV) chains, respectively. The alpha 5(IV) chain has less sequence identity with the putative bovine alpha 3(IV) and alpha 4(IV) chains. Antiserum against an alpha 5(IV) synthetic peptide stained a polypeptide chain of about 185 kDa by immunoblot analysis and immunolocalization of the chain in human kidney was almost completely restricted to the glomerulus. The gene was assigned to the Xq22 locus by somatic cell hybrids and in situ hybridization. This may be identical or close to the locus of the X chromosome-linked Alport syndrome that is believed to be a type IV collagen disease. |
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Biocenter, University of Oulu, Finland |
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English |
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0027-8424 |
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| Notes |
PMID:1689491 |
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no |
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Equine Behaviour @ team @ |
Serial |
5291 |
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Harvey, P.H.; Clutton-Brock, T.H.; Mace, G.M. |
| Title |
Brain size and ecology in small mammals and primates |
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Journal Article |
| Year |
1980 |
Publication |
Proceedings of the National Academy of Sciences |
Abbreviated Journal |
PNAS |
| Volume |
77 |
Issue |
7 |
Pages |
4387-4389 |
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Equine Behaviour @ team @ |
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5456 |
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