European checkerspots (Melitaeini: Lepidoptera,Nymphalidae) are not aposematic – the point of view of great tits (Parus major)

相似文献   

Folding of beta-hairpins

Identification of the factors governing the formation of beta-structure independently of the rest of the protein is important for understanding the folding process of protein into a unique native structure. It has been shown that some beta-hairpins can fold autonomously into native-like structures, either in aqueous solution or in the presence of an organic co-solvent. Our aim is to review recent theoretical and experimental studies of folding of beta-structures.     

The difference between protein structures that are obtained by X-ray analysis and magnetic resonance spectroscopy

We have analyzed the proteins whose structures were determined both by X-ray analysis (X-ray) and nuclear magnetic resonance (NMR) on condition that these structures do not differ greatly when spatially superimposed on each other (61 pairs of protein structures). Atom-atomic contacts (contact distances varied from 2 to 8 A) have been analyzed and it has been found that NMR structures (in comparison with X-ray ones) have more contacts in the range below 3.5 A and above 5.5 A. In the case of residue-residue contacts NMR structures have more contacts below 3 A and between 4.5 and 6.5 A. At all the other contact distances analyzed the X-ray structures have more contacts. The difference in the number of atom-atomic and residue-residue contacts is greater for internal residues, that are concealed from water, as compared to the surface residues. The other, not less important difference deals with the number of hydrogen bonds in the main chain: it is larger for the X-ray structures. The correlation between the hydrogen bonds identified in the structures obtained by both methods is no more than 32%. The consideration of a complete set of protein structures obtained by NMR results in the fact that the number of hydrogen bonds grows 1.2 times as compared to those obtained with the X-ray analysis, whereas the correlation increases only by 65%. We have also demonstrated that alpha-helices in the NMR structures are more distorted in comparison with the ideal alpha-helix, than alpha-helices in the X-ray structures.     

On prediction of folding nuclei in globular proteins

The approach described in this paper on the prediction of folding nuclei in globular proteins with known three dimensional structures is based on a search of the lowest saddle points through the barrier separating the unfolded state from the native structure on the free-energy landscape of protein chain. This search is performed by a dynamic programming method. Comparison of theoretical results with experimental data on the folding nuclei of two dozen of proteins shows that our model provides good phi value predictions for proteins whose structures have been determined by X-ray analysis, with a less limited success for proteins whose structures have been determined by NMR techniques only. Consideration of a full ensemble of transition states results in more successful prediction than consideration of only the transition states with the minimal free energy. In conclusion we have predicted the localization of folding nuclei for three dimensional protein structures for which kinetics of folding is studied now but the localization of folding nuclei is still unknown.     

Formation of spatial structure of RNA molecules

In this review we consider several experimental and theoretical approaches for investigation of RNA folding and determination of nucleotides that play an important role upon folding of such molecules as tRNA and several classes of ribozymes. It has been shown that nucleotides in the D- and T-loop regions are the last to be involved in tRNA structure or they are not included in the folding nucleus of tRNA. Using the specially elaborated method SHAPE it has been demonstrated that the model of hierarchical folding which was recognized for a long time is not correct for tRNA folding. In the second part of the given review the algorithms and programs used for the prediction of secondary structures of RNA as well as for modeling of RNA folding are considered.     

Radius of gyration is indicator of compactness of protein structure

Search and study of the general principles that govern kinetics and thermodynamics of protein folding generate a new insight into the factors controlling this process. Statistical analysis of radii of gyration for 3769 protein structures from four general structural classes (all-alpha, all-beta, alpha/beta, alpha + beta) demonstrates that each class of proteins has its own class-specific radius of gyration, which determines compactness of protein structures: alpha-proteins have the largest radius of gyration. This indicates that they are less tightly packed than beta- and alpha + beta-proteins. Finally, alpha/beta-proteins are the most tightly packed proteins with the least radius of gyration. It should be underlined that radius of gyration normalized on the radius of gyration of ball with the same volume, is independent of the length in comparison with such parameters as compactness and number of contacts per residue.     

ONTOGENETIC NICHE SHIFT IN THE BRACHIOPOD TEREBRATALIA TRANSVERSA: RELATIONSHIP BETWEEN THE LOSS OF ROTATION ABILITY AND ALLOMETRIC GROWTH

Abstract: Many articulated brachiopods experience marked life habit variations during ontogeny because they experience their fluid environment at successively higher Reynolds numbers, and they can change the configuration of their inhalant and exhalant flows as body size increases. We show that the extant brachiopod Terebratalia transversa undergoes a substantial ontogenetic change in reorientation governed by rotation around the pedicle. T. transversa′s reorientation angle (maximum ability to rotate on the pedicle) decreases during ontogeny, from 180 degrees in juveniles to 10–20 degrees in individuals exceeding 5 mm, to complete cessation of rotation in individuals larger than 10 mm. Rotation ability is substantially reduced after T. transversa achieves the adult lophophore configuration and preferred orientation with respect to ambient water currents at a length of 2.5–5 mm. We hypothesize that the rotation angle of T. transversa is determined mainly by the position of ventral and dorsal points of attachment of dorsal pedicle muscles relative to the pedicle. T. transversa shows a close correlation between the ontogenetic change in reorientation angle and ontogeny of morphological traits that are related to points of attachment of dorsal pedicle muscles, although other morphological features can also limit rotation in the adult stage. The major morphological change in cardinalia shape and the observed reduction of rotation affect individuals 2.5–10 mm in length. The position of ventral insertions of dorsal pedicle muscles remains constant, but contraction of dorsal pedicle muscles is functionally handicapped because dorsal insertions shift away from the valve midline, rise above the dorsal valve floor, and become limited by a wide cardinal process early in ontogeny (<5 mm). The rate of increase of cardinal process width and of distance between dorsal pedicle muscle scars substantially decreases in the subadult stage (5–10 mm), and most of the cardinalia shell traits grow nearly isometrically in the adult stage (>10 mm). T. transversa attains smaller shell length in crevices than on exposed substrates. The proportion of small‐sized individuals and population density is lower on exposed substrates than in crevices, indicating higher juvenile mortality on substrates prone to grazing and physical disturbance. The loss of reorientation ability can be a consequence of morphological changes that strengthen substrate attachment and maximize protection against biotic or physical disturbance (1) by minimizing torques around the pedicle axis and/or (2) by shifting energy investments into attachment strength at the expense of the cost involved in reorientation.     

Optimal relationship between average conformational entropy and average energy of interactions between residues for fast protein folding

Based on the known experimental data and using the theoretical modeling of protein folding, we demonstrate that there exists an optimal relationship between the average conformational entropy and the average energy of contacts per residue, that is an entropy capacity, for fast protein folding. Statistical analysis of conformational entropy and the number of contacts per residue for 5829 protein structures from four general structural classes (all-alpha, all-beta, +/-/beta, alpha+beta) demonstrates that each class of proteins has its own class-specific average number of contacts and average conformational entropy per residue. These class-specific features determine the folding rates: a proteins are the fastest folding proteins, then follow beta and alpha+beta proteins, and finally alpha/beta proteins are the slowest ones.     

Sensitivity of the folding pathway to the details of amino acid sequence

Experimental data on the structure of transition state demonstrate that the proteins with the same topology as a rule have similar folding nuclei (the structured formed part of the transition state). In this review we discuss the experimental works which show that the position of folding nuclei is different among proteins with the same topology. These facts underline that the folding pathway is sensitive to the details of amino-acid sequence.