Book ChapterDOI
Hydrogen exchange in proteins.
Aase Hvidt,Sigurd O. Nielsen +1 more
TLDR
Quantitative measurements of the rate of hydrogen exchange in a given protein, under specified experimental conditions, provide a multiparameter characterization of the protein conformation (or distribution of conformations) present under these conditions.Abstract:
Publisher Summary The chapter reviews the results obtained from measurements of hydrogen exchange (H–H, H–D, and H–T) in proteins and related compounds. The slowness of the rate of hydrogen exchange in a protein, relative to the exchange rate observed with simple peptides under the same experimental conditions is closely related to the conformation of the protein molecule in aqueous solution. Quantitative measurements of the rate of hydrogen exchange in a given protein, under specified experimental conditions, provide a multiparameter characterization of the protein conformation (or distribution of conformations) present under these conditions. Moreover, the chapter discusses the experimental techniques that have been used to measure quantitatively the rate of hydrogen exchange. The chapter also discusses arguments that support case, as the mechanism of exchange of the slowly exchanging hydrogen atoms.read more
Citations
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Journal ArticleDOI
Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures
Jilie Kong,Shaoning Yu +1 more
TL;DR: This review introduces the recent developments in Fourier transform infrared (FTIR) spectroscopy technique and its applications to protein structural studies.
Journal ArticleDOI
From Levinthal to pathways to funnels
Ken A. Dill,Hue Sun Chan +1 more
TL;DR: The general energy landscape picture provides a conceptual framework for understanding both two-state and multi-state folding kinetics and hopes to learn much more about the real shapes of protein folding landscapes.
Book ChapterDOI
Stability of Proteins Small Globular Proteins
TL;DR: The chapter discusses the stability of proteins and presents the results obtained on small compact globular proteins, which represent one single cooperative system, and the temperature-induced changes in protein, denaturational and predenaturational changes inprotein, thermodynamics of protein unfolding, and thermodynamic properties of protein.
Book ChapterDOI
Protein denaturation. C. Theoretical models for the mechanism of denaturation.
TL;DR: This chapter reviews theoretical models that might be constructed and equations that may be derived from them to understand the process of protein denaturation and finds that they can be predicted semiquantitatively.
Journal ArticleDOI
Hydrogen exchange and structural dynamics of proteins and nucleic acids
TL;DR: Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid.
References
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Journal ArticleDOI
Use of glass electrodes to measure acidities in deuterium oxide1,2
Paul K. Glasoe,F. A. Long +1 more
TL;DR: In this article, a pH meter reading in D/sub 2/O solutions was 0-40 pH unit lower than in H/sub O solutions, attributed to the glass electrode.
Journal ArticleDOI
A three-dimensional model of the myoglobin molecule obtained by x-ray analysis.
TL;DR: Kendrew et al. as mentioned in this paper used Max Perutz's technique to produce the first 3D images of any protein -myoglobin, the protein used by muscles to store oxygen.
Journal ArticleDOI
Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis
Journal ArticleDOI
The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands1
T. Miyazawa,E. R. Blout +1 more
Book ChapterDOI
Ultraviolet spectra Of Proteins and Amino Acids
TL;DR: This chapter reviews that the simplest way of accounting for the absorption spectrum of a protein is as the sum of the spectra of its components, and discusses that the failure of perfect additivity of the component absorptivities affords the possibility of obtaining structural information about proteins.