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Protein Folding
  • Language: en
  • Pages: 580

Protein Folding

Protein Folding aims to collect the most important information in the field of protein folding and probes the main principles that govern formation of the three-dimensional structure of a protein from a nascent polypeptide chain, as well as how the functional properties appear. This text is organized into three sections and consists of 15 chapters. After an introductory chapter where the main problems of protein folding are considered at the cellular level in the context of protein biosynthesis, the discussion turns to the conformation of native globular proteins. Definitions and rules of nomenclature are given, including the structural organization of globular proteins deduced from X-ray cr...

Protein Folding
  • Language: en
  • Pages: 63

Protein Folding

  • Type: Book
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  • Published: 2019-02-25
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  • Publisher: Springer

This snapshot volume is designed to provide a smooth entry into the field of protein folding. Presented in a concise manner, each section introduces key concepts while providing a brief overview of the relevant literature. Outlook subsections will pinpoint specific aspects related to emerging methodologies, concepts and trends.

Protein Folding
  • Language: en
  • Pages: 128

Protein Folding

Discusses the molecular mechanisms controlling protein folding in vivo and in vitro.

Protein Folding
  • Language: en
  • Pages: 294

Protein Folding

Proteins are one of the most basic components of all living cells and therefore serve a vital purpose in the cells of animals, plants and bacteria. They are comprised of chains of amino acids, which are held together by ribosome. These chains have many different patterns, which are known as `folds.' These folds are complicated, and therefore susceptible to irregularities that are known to be the source of many diseases. Cystic fibrosis, mad cow disease, Alzheimer's disease, emphysema and others are all initiated by improper protein folds. It is clear that, improving our understanding of protein folding is a key to fighting these diseases. This book presents recently performed research from around the world on this important subject.

Protein Folding, Misfolding and Aggregation
  • Language: en
  • Pages: 290

Protein Folding, Misfolding and Aggregation

Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods h.

Protein Folding
  • Language: en
  • Pages: 55

Protein Folding

  • Type: Book
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  • Published: 2014-12-01
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  • Publisher: Springer

The book will discuss classes of proteins and their folding, as well as the involvement of bioinformatics in solving the protein folding problem. In vivo and in vitro folding mechanisms are examined, as well as the failures of in vitro folding, a mechanism helpful in understanding disease caused by misfolding. The role of energy landscapes is also discussed and the computational approaches to these landscapes.

Protein Folding, Evolution and Design
  • Language: en
  • Pages: 347

Protein Folding, Evolution and Design

  • Type: Book
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  • Published: 2001-09-25
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  • Publisher: IOS Press

This book presents the results of broad interdisciplinary effort to study proteins in physical and evolutionary prospective. Among authors are physicists, computational chemists, crystallographers and evolutionary biologists. New experimental and theoretical developments ''from molecules to cells'' are presented providing a broad picture of modern biophysical chemistry

The Protein Folding Problem
  • Language: en
  • Pages: 203

The Protein Folding Problem

  • Type: Book
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  • Published: 2019-06-21
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  • Publisher: Routledge

Proteins in living systems carry out a great variety of specific functions, each of which depends on the precise three-dimensional structure of a particular protein. Proteins are synthesized in the form of a flexible polypeptide chain that is capable of assuming a vast number of configurations; the transformation of this chain into a specific, relatively rigid three-dimensional structure is called folding--a remarkable process of self-organization. It is known that the amino acid sequences of some proteins have sufficient information to determine their three-dimensional structures. There are other proteins whose folding requires additional information beyond that found in the sequence of the...

The Protein Folding Problem and Tertiary Structure Prediction
  • Language: en
  • Pages: 585

The Protein Folding Problem and Tertiary Structure Prediction

A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology...

Protein Folding Protocols
  • Language: en
  • Pages: 332

Protein Folding Protocols

Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences.