Conformational proteomics of macromolecular architecture : approaching the structure of large molecular assemblies and their mechanisms of action / R. Holland Cheng & Lena Hammar, editors.

Contributor(s):

Material type: Text

text

Media type:

computer

Carrier type:

online resource

ISBN:

9812562648
9789812562647
1281347698
9781281347695

Subject(s): Genre/Form:

Electronic books.

Additional physical formats: Print version:: Conformational proteomics of macromolecular architecture.DDC classification:

547.7 22

LOC classification:

QP801.P64 C66 2004eb

NLM classification:

QU 55

Online resources:

EBSCOhost

Contents:

Conformational Proteomics of Macromolecular Architecture: Approaching the Structure of Large Molecular Assemblies and Their Mechanisms of Action; PREFACE; Dynamic Architectures; The Theory of Quasi-equivalence; Approaching Large Assemblies in Membranes; Protein Shuttle; Molecular Machines; Conformational Proteomics; Acknowledgements; CONTENTS; Chapter 1. Early Theories of Virus Structure; Chapter 2. Quasi-Equivalence and Adaptability in Living Molecular Assemblies; Chapter 3. The Role of Disordered Segments in Viral Coat Proteins.

Summary: Biological processes involving large macromolecular assemblies arethought to be a dynamic consequence of cooperativity andmetastability. The folding of a peptide chain creates localenvironments from which "activity" can emerge. In the same way, theassembly of large molecular complexes creates dynamic features thatwould only be feasible in a large construct. The biologicalimplications of such adaptation will be explored as it applies to thestatic quasisymmetry situations, as well as to the dynamics ofstructural transitions. The current wealth of solved high-resolutioncomplex structures makes th

Holdings ( 1 )
Title notes ( 5 )

Holdings
Item type	Current library	Collection	Call number	Status	Date due	Barcode	Item holds
eBook	e-Library	EBSCO Science		Available

Total holds: 0

Includes bibliographical references and index.

Print version record.

Biological processes involving large macromolecular assemblies arethought to be a dynamic consequence of cooperativity andmetastability. The folding of a peptide chain creates localenvironments from which "activity" can emerge. In the same way, theassembly of large molecular complexes creates dynamic features thatwould only be feasible in a large construct. The biologicalimplications of such adaptation will be explored as it applies to thestatic quasisymmetry situations, as well as to the dynamics ofstructural transitions. The current wealth of solved high-resolutioncomplex structures makes th

Added to collection customer.56279.3