1.

Record Nr.

UNISA990001608070203316

Autore

GALEOTTI, Serio

Titolo

Un governo scelto dal popolo : il governo di legislatura : contributo per una grande riforma istituzionale / Serio Galeotti

Pubbl/distr/stampa

Milano : Giuffré, 1984

ISBN

88-14-00197-9

Descrizione fisica

176 p. ; 24 cm.

Disciplina

320.445

Collocazione

IX B 640

Lingua di pubblicazione

Italiano

Formato

Materiale a stampa

Livello bibliografico

Monografia

2.

Record Nr.

UNINA9910461561803321

Titolo

The biology of squat lobsters [[electronic resource] /] / editors, Gary C.B. Poore, Shane T. Ahyong, Joanne Taylor

Pubbl/distr/stampa

Australia, : CSIRO Pub., 2011

ISBN

1-283-39521-5

9786613395214

0-643-10434-8

Descrizione fisica

1 online resource (382 p.)

Altri autori (Persone)

PooreGary C. B

AhyongShane T

TaylorJoAnne

Disciplina

595.384

Soggetti

Lobsters

Decapoda (Crustacea)

Electronic books.

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.



Nota di bibliografia

Includes bibliographical references and indexes.

Nota di contenuto

Kareen E. Schnabel, Patricia Cabezas, Anna McCallum, Enrique Macpherson, Shane T. Ahyong and Keiji Baba6Ecology, physiology, feeding and trophic role of squat lobsters; Gustavo A. Lovrich and Martin Thiel; 7Agonistic behaviour and reproductive biology of squat lobsters; Martin Thiel and Gustavo A. Lovrich; 8Squat lobsters as symbionts and in chemo-autotrophic environments; J. Antonio Baeza; 9Parasites and other symbionts of squat lobsters; Christopher B. Boyko and Jason D. Williams; 10Squat lobster fisheries; Ingo S. Wehrtmann and Enzo Acuña; Colour plates; General index; Taxonomic index

Sommario/riassunto

Brings together current thinking on this diverse group of marine decapod crustaceans.

3.

Record Nr.

UNINA9910557509403321

Autore

Simon István

Titolo

Functionally Relevant Macromolecular Interactions of Disordered Proteins

Pubbl/distr/stampa

Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2020

Descrizione fisica

1 online resource (520 p.)

Soggetti

Biology, life sciences

Research and information: general

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Sommario/riassunto

Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999. First, it was generally thought for more than a decade that disordered proteins or disordered parts of proteins have different amino acid compositions than folded proteins, and various prediction methods were developed based on this principle. These



methods were suitable for distinguishing between the disordered (unstructured) and structured proteins known at that time. In addition, they could predict the site where a folded protein binds to the disordered part of a protein, shaping the latter into a well-defined 3D structure. Recently, however, evidence has emerged for a new type of disordered protein family whose members can undergo coupled folding and binding without the involvement of any folded proteins. Instead, they interact with each other, stabilizing their structure via "mutual synergistic folding" and, surprisingly, they exhibit the same residue composition as the folded protein. Increasingly more examples have been found where disordered proteins interact with non-protein macromolecules, adding to the already large variety of protein-protein interactions. There is also a very new phenomenon when proteins are involved in phase separation, which can represent a weak but functionally important macromolecular interaction. These phenomena are presented and discussed in the chapters of this book.