Journal ArticleDOI
The Interpretation of Infrared Dichroism in Fibrous Protein Structures
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In this article, the relationship between transition moment direction and dichroic ratio was derived for perfectly and imperfectly oriented fibers, and the effects of reflection losses, form dichroism, and convergence were considered.Abstract:
The increasing use of infrared dichroism measurements in studying the molecular structure of fibrous proteins necessitates a critical examination of its interpretation. Relationships between transition moment direction and dichroic ratio are derived for perfectly and imperfectly oriented fibers, and the effects of reflection losses, form dichroism, and convergence are considered. Uncertainties in the assignment of the transition moment directions associated with the principal vibrations of the —CO·NH— group are discussed.read more
Citations
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Journal ArticleDOI
Two-Dimensional Infrared (2D IR) Spectroscopy: Theory and Applications
TL;DR: In this paper, a two-dimensional infrared (2D IR) spectroscopy was proposed for elucidating various chemical interactions among functional groups, which simplifies complex spectra consisting of many overlapped peaks and enhances spectral resolution by spreading peaks over the second dimension.
Journal ArticleDOI
The molecular structure of collagen.
Alexander Rich,Francis Crick +1 more
TL;DR: A demonstration that, given certain assumptions, only two basic types of structures are possible for collagen, and detailed work on the coordinates and Fourier transforms of one of these models (collagen II), and a comparison between these predictions and the observed X-ray diffraction data.
Journal ArticleDOI
Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes.
TL;DR: Preparation of pure protein ¢lms in an aqueous environment by adsorption on the IRE and Observation of a¬lm in situ by external re£ection.
Book ChapterDOI
Infrared spectra of high polymers
TL;DR: In this article, the spectral properties of polyethylene terephthalate and three deuterated analogs have been obtained in the region of 70 to 3600 cm-i, polarized spectra having been obtained down to 330 cm-l. This assignment suggests a modification of the proposed chain structure of this polymer.
Book ChapterDOI
Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds.
TL;DR: In this article, the authors reviewed the basic knowledge accumulated over the last twenty years on the different vibrations of polypeptides and pointed out that interpretation of the results still needs caution.
References
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Journal ArticleDOI
The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.
TL;DR: This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.
Journal ArticleDOI
Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets
Linus Pauling,Robert B. Corey +1 more
TL;DR: In recent papers, several configurations of polypeptide chains with interatomic distances, bond angles, and other structural features as indicated by the studies in these Laboratories of the structure of crystals of amino acids, simple peptides, and related substances are described.
Journal ArticleDOI
Atomic coordinates and structure factors for two helical configurations of polypeptide chains.
Linus Pauling,Robert B. Corey +1 more
TL;DR: The discovery of two helical configurations of the polypeptide chain that satisfy the conditions for diffraction of x-rays in the equatorial direction are reported.
Journal ArticleDOI
Polypeptide chain configurations in crystalline proteins
TL;DR: A systematic survey has been made of chain models which conform to established bond lengths and angles, and which are held in a folded form by N—H—O bonds, indicating that a further intensive study of these proteins, and in particular of myoglobin which has promising features of simplicity, may lead to a determination of the chain structure.