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Abstrak :
Diajukan sebuah model yang menjelaskan mekanisme pembentukan gerak pada protein berdasarkan interaksi-interaksi materi dengan pendekatan lagrangian. Sumber non-linier yang disuntikan direpresentasikan oleh lagrangian medan elektromagnetik. Pelipatan protein terjadi karena sumber nonlinier merambat melalui badan protein. Perambatan sumber non-linier melalui badan protein, dapat membuat transisi protein dari bentuk metastabil ke keadaan dasar. ......A model to describe the mechanism of conformational dynamics in protein based on matter interactions using lagrangian approach is proposed. Nonlinear sources injected are represented by electromagnetic feld lagrangian. Protein folding is caused by nonlinear source propagate through the protein backbone. Propagation of nonlinear source through the bakcbobe of the protein, can mediate the transition of a protein from metastable conformation to its ground state.

Abstrak :
Diajukan sebuah model yang menjelaskan mekanisme pembentukan gerak pada protein berdasarkan interaksi-interaksi materi dengan menggunakan pen¬dekatan lagrangian dan perusakan simetri. Perubahan bentuk protein dan sumber non-linier yang disuntikan direpresentasikan oleh lagrangian boson dengan tambahan interaksi φ4 sebagai sumber gangguan. Metode path in¬tegral digunakan untuk menghitung sifat mekanika statistik-nya. ......A model to describe the mechanism of conformational dynamics in protein based on matter interactions using lagrangian approach and imposing certain symmetry breaking is proposed. Both conformation changes of proteins and the injected non-linear sources are represented by the bosonic lagrangian with an additional φ4 interaction for the sources. The path integral method is used to calculate its statistical mechanic properties.

Abstrak :
This volume has a strong focus on homo-oligomerization, which is surprisingly common. However, protein function is so often linked to both homo- and hetero-oligomerization and many heterologous interactions likely evolved from homologous interaction, so this volume also covers many aspects of hetero-oligomerization.

Abstrak :
The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Abstrak :
In this volume, Peter Tompa and Monika Fuxreiter have assembled a series of papers that address the issue of fuzziness in molecular interactions. These papers provide a broad overview of the phenomenon of fuzziness and provide compelling examples of the central role played by fuzzy interactions in regulation of cellular signaling processes and in viral infectivity. These contributions summarize the current state of knowledge in this new field and will undoubtedly stimulate future research that will further advance our understanding of fuzziness and its role in biomolecular interactions.

Abstrak :
While significant progress has been made in the past decade, the current understanding of protein aggregation and its consequences is still immature. Aggregation of Therapeutic Proteins provides an up-to-date resource on protein aggregation and its consequences, and available methods to control or slow down the aggregation process. This book also covers an overview on the causes, consequences, characterization, and control of the aggregation of therapeutic proteins. The knowledge in this book will help pharmaceutical scientists in the development of therapeutic proteins, and also instigate further scientific investigations in this area.