Unfolded Proteins, Volume 62

1st Edition

Print ISBN: 9780124013711
eBook ISBN: 9780080524528
Imprint: Academic Press
Published Date: 21st October 2002
Page Count: 398
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A variety of complementary techniques and approaches have been used to characterize peptide and protein unfolding induced by temperature, pressure, and solvent. Volume 62, Unfolded Proteins, assembles these complementary views to develop a more complete picture of denatured peptides and proteins. The unifying observation common to all chapters is the detection of preferred backbone confirmations in experimentally accessible unfolded states.

Key Features

@introbul:Key Features @bul:* Peptide and protein unfolding induced by temperature, pressure, and solvent

  • Denatured peptides and proteins
  • Detection of preferred backbone confirmations in experimentally accessible unfolded states


Biochemists, molecular and cell biologists, and biotechnologists

Table of Contents

The Expanded Denatured State: An Ensemble of Conformations Trapped in a Locally Encoded Topological Space. Identification and Functions of Usefully Disordered Proteins. Unfolded Proteins Studied by Raman Optical Activity. What Can Fluorescence Correlation Spectroscopy Tell Us About Unfolded Proteins. Unfolded Peptides and Proteins Studied with Infrared Absorption and Vibrational Circular Dichroism Spectra. Is Polyproline II a Major Backbone Conformation in Unfolded Protein. Toward a Taxonomy of the Denatured State: Small Angle Scattering Studies of Unfolded Proteins. Determinants of the Polyproline II Helix from Modeling Studies. Hydration Theory for Molecular Biophysics. Insights Into the Structure and Dynamics of Unfolded Proteins from Nuclear Magnetic Resonance. A New Perspective on Unfolded Proteins.


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© Academic Press 2003
Academic Press
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@from:PRAISE FOR THE SERIES @qu:"The authority, originality, and editing of the reviews are first class." @source:—NATURE @qu:"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists." @source:—JOURNAL OF THE AMERICAN CHEMICAL SOCIETY