Theory of helix-coil transitions in biopolymers statistical mechanical theory of order-disorder transitions in biological macromolecules by Douglas Poland

Cover of: Theory of helix-coil transitions in biopolymers | Douglas Poland

Published by Academic Press in New York .

Written in English

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Subjects:

  • Biopolymers.,
  • Biochemistry.,
  • Statistical mechanics.

Edition Notes

Includes bibliographies.

Book details

Statementby Douglas Poland and Harold A. Scheraga.
SeriesMolecular biology
ContributionsScheraga, Harold A., 1921-
Classifications
LC ClassificationsQD381 .P6
The Physical Object
Paginationxvii, 797 p.
Number of Pages797
ID Numbers
Open LibraryOL5754541M
LC Control Number71091417

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Buy Theory of Helix-Coil Transitions in Biopolymers;: Statistical Mechanical Theory of Order-Disorder Transitions in Biological Macromolecules on FREE SHIPPING on qualified  › Books › Science & Math › Biological Sciences.

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Every book that is provided in better way and utterance will be expected by many :// Theory of helix-coil transitions in biopolymers; statistical mechanical theory of order-disorder transitions in biological macromolecules, EARLY STUDIES OF HELIX–COIL TRANSITIONS.

The early statistical mechanical treatment of the helix–coil transition is summarized in a book that provided the various theoretical approaches and also reprinted the seminal Theory of helix-coil transitions in biopolymers book in which these approaches were described.

63 The factors relating to the question of a phase transition in polyamino acids 64 and polynucleotides, 65 the kinetics of Poland, Douglas. and Scheraga, Harold A. Theory of helix-coil transitions in biopolymers; statistical mechanical theory of order-disorder transitions in biological macromolecules, by Douglas Poland and Harold A.

Scheraga Academic Press New York Australian/Harvard Citation. Poland, :// Biopolymers Volume 1, Issue 1. Article. Theory of the helix–coil transition in DNA considered as a copolymer. Theory of helix-coil transitions in biopolymers book Shneior Lifson. Weizmann Institute of Science, Rehovot, Israel.

Search for more papers by this author. Shneior Lifson. Weizmann Institute of Science, Rehovot, :// Find helpful customer reviews and review ratings for Theory of Helix-Coil Transitions in Biopolymers;: Statistical Mechanical Theory of Order-Disorder Transitions in Biological Macromolecules at Read honest and unbiased product reviews from our ://   Helical conformations, such as the α-helix in polypeptides and the double helix in DNA, are common structural elements in biopolymers.

As the temperature is raised or the p H is changed to extremes of acidity or alkalinity, the helix becomes disordered into a random coil state.

The helix–coil transition has been extensively studied, both experimentally and theoretically, as a model for   The kinetics of helix-coil transitions in polypeptides like POlY-L -glutamic acid and its derivatives or other similar structural transformations in biopolymers like the polyproline I-II transition, etc.

has been the sub­ ject of numerous experimental (e. g., Refs. ) and theoretica studies. Most of the experiments [varia­~hp/P_ABBinder_JCPpdf. TRANSITIONS IN BIOPOLYMERS That is, a one-dimensional Ising model can be used to Zimm and coworkers (2), Hill (3) The helix-coil characterize many properties of a macromolecular transition process in dilute solutions.

and Applequist (4) have extended the Ising lattice model so to include multiple-chain molecular assemblies. transition in Theory of helix-coil transitions in biopolymers; statistical mechanical theory of order-disorder transitions in biological macromolecules Responsibility by Douglas Poland and Harold A.

:// Biopolymers. Vol Issue 2. Article. Helix–coil transition in heterogeneous DNA. Marshall Fixman. Department of Chemistry, Yale University, New Haven, Connecticut Search for more papers by this author. Marshall Fixman. Department of Chemistry, Yale University, New Haven, Connecticut A dynamical theory of the helix-coil transitions in polypeptides and in polynucleotide-polynucleotide complexes with arbitrary lengths is presented, which uses an Ising model in a static magnetic field.

From time-dependent spin correlations calculated, it is shown that quite similar modes of the helix-coil transitions are mainly contributing to all experiments of NMR, tritium-hydrogen exchange   A dynamical theory of the helix‐coil transitions in polypeptides and in polynucleotide‐polynucleotide complexes with arbitrary lengths is presented, which uses an Ising model in a static magnetic :// This chapter reviews the elementary statistical properties of a single polymer chain in solvents of different nature.

Starting with the ideal random coil conformation and its tension–elongation relation, the excluded-volume effect is introduced to study the swelling and collapse of a random :// For the Ising model, the nature of this critical behavior has been extensively discussed, in particular to analyze the helix-coil transition in biopolymers [54,55,56,57,58,59,60, 61].

The effect   theory of the helix-coil transition must be able to dupli- cate. There is a substantial collection of literature on the kinetics of the helix-coil transition employing the kinetic version of the Zimm-Bragg14 theory in single-chain poly- peptides.

Basically the approaches involve the solution   Molecular theory of the helix-coil transition in polyamino acids. Explanation of the different conformational behavior of valine, isoleucine, and leucine in aqueous solution. Biopolymers23 (10), DOI: /bip MeltSim is a statistical-mechanical program for calculating melting (denaturation) curves (derivative profiles) and maps of DNA, from genes to genomes.

In Theory of Helix-Coil Transitions in Biopolymers. Academic Press, New York. (book out of print) Poland, D. Biopolymers   Time correlation function theory of the dynamics of helix–coil transitions. The Journal of Chemical Physics73 (3), DOI: / Takayuki Sano, Tatsuya Yasunaga.

Kinetics of helix-coil transition of polypeptides in solution by the relaxation methods. Biophysical Chemistry11 (), DOI: / Helix–coil transition in heterogeneous DNA Helix–coil transition in heterogeneous DNA Fixman, Marshall The broadening of a helix–coil transition due to base pair heterogeneity is calculated on the basis of a cumulant perturbation expansion in the quasi‐grand ensemble.

In this ensemble the fictitious, homogeneous chain, to which the perturbation is referred 1. Author(s): Poland,Douglas; Scheraga,Harold Abraham, Title(s): Theory of helix-coil transitions in biopolymers; statistical mechanical theory of order-disorder transitions in biological macromolecules, by Douglas Poland and Harold A.

Scheraga. Country of Publication: United States Publisher: New York, Academic Press, 1. Introduction. The helix–coil transition received early attention as a simplified model for conformational changes in globular subsequent analysis indicated that such a simplified model cannot capture the cooperative features of the folding/unfolding transition of globular proteins, the recent revived interest in helix–coil transitions has focused on the intrinsic The results for parameter set A are: for polyglycine, the helix‐coil transition temperature is °C, at which ΔH8 = − kcal/mole residue, ΔS8 = − eu, and σ = 10−; for poly   Statistical thermodynamics of helix–coil transitions in biopolymers American Journal of Phys (); / Theory of the One-Dimensional Phase Transition in Polypeptide / Enthalpies of helix–coil transitions in polypeptides Enthalpies of helix–coil transitions in polypeptides Karasz, F.

E.; Gajnos, G. Certain discrepancies in measured heats of helix–coil transitions in polypeptides are examined in terms of the theory of the effect of solvent composition on transition temperatures and heats in such :// Helix-coil transitions in polyalanine molecules of length 10 are studied by multicanonical Monte Carlo simulations.

The solvation effects are included by either a distance-dependent dielectric permittivity or by a term that is proportional to the solvent-accessible surface area of the peptide. We found a strong dependence of the characteristics of the helix-coil transition from the details of (02)   D.

Poland and H. Scheraga, Theory of Helix-Coil Transitions in Biopolymers (Academic Press, New York, ). A modified version of the force field of Jorgensen and Tirado-Rives (24) was used, which included a kcal/mol barrier to torsional rotation about the triple bond as inferred from gas-phase spectroscopy (25).

Previously, the Zimm–Bragg parameters s and σ for the helix–coil transition in polyglycine and poly‐l‐alanine were calculated in terms of molecular quantities. These calculations are extended here to take into account the effects of water as the solvent and are analyzed to deduce the relative importance of the various interaction terms for the helix–coil ://   The Generalized Model of Polypeptide Chain Describing the Helix-Coil Transition in Biopolym_专业资料。 In this paper we summarize some results of our theoretical investigations of helix-coil transition both in single-strand (polypeptides) and two-strand (polynucleotides) ://   The structural and mechanical properties of gels formed from biopolymers are discussed both in terms of the techniques used to characterise these systems, and in terms of the systems themselves.

The techniques included are spectroscopic, chiroptical and scattering methods, optical and electron microscopy, thermodynamic and kinetic methods and    and ga, Theory of helix-coil transitions in biopolymers. Academic Press (). rg and ov, Statistical Physics of Macromolecules. AIP Press ().

andOn the theory of helix-coil transition  › 百度文库 › 互联网. Brändén, C.-I. & Tooze, J. () Introduction to protein structure, 2nd ed., Garland Publishing, Hamden, CT. Google Scholar   Solution effects and the order of the helix–coil transition in polyalanine J.

Chem. Phys.(); / Solvent effects on conformational dynamics of proteins: Cytochrome c in a dried trehalose film J. Chem. Phys.(); / Statistical thermodynamics of helix–coil transitions in ~rudi/reprints/ The quasi-equilibrium evolution of the helical fraction occurring in a biopolymer network (gelatin gel) under an applied stress has been investigated by observing modulation in its optical activity.

Its variation with the imposed chain extension is distinctly nonmonotonic and corresponds to the transition of initially coiled strands to induced left-handed ://(06) Theory of the effects of concentration and chain length on helix-coil equilibria in two-stranded nucleic acids.

Chem. Phys.,J. Rifkind and J. Applequist. The helix interruption constant for poly- L-glutamic acid from the pressure dependence of optical rotation. This chapter presents some important nongelling binary associating mixtures.

Throughout this chapter, we assume the pairwise association of reactive groups, the strength of which can be expressed in terms of the three association constants for AA, BB, and AB association. We apply the general theory presented in Chapter 5 to specific systems, such as dimerization, linear association, side of informational interaction in analyzing helix-coil transitions in biopolymers having a helical secondary structure.

SOME PROBLEMS OF THE STATISTICAL THEORY OF BIOPOLYMERS fibrous proteins). The volume interaction between the links of a flexible chain entangled into a loose random coil involves weaker forces not generally having   & () Theory of Helix-Coil Transitions in Biopolymers, Academic Press, New   theory of cooperative transitions in protein molecules why denaturation of globular protein is a 1st-order phase-transition biopolymers 28 (10): oct finkelstein av, shakhnovich ei theory of cooperative transitions in protein molecules phase-diagram for a protein molecule in solution biopolymers 28 (10): oct.

to study helix-coil transitions of polynucleotides. The theory predicts the existence of hysteresis when the electrostatic interaction parameter is large compared to the thermal energy.

The theory is applied to the acid-base titration of poly(A).2 poly(U). INTRODUCTION The influence of cooperativity on conformational changes in biopolymers  Isotope exchange experiments in the study of the helical conformation of a polypeptide suggest that the rate constant of the helix—coil change of a unit depends on its location and that it is unfolding curves for short peptides to helix-coil transition theory, as regards the problem of deter- mining accurate helical propensities.

One is to find out how well standard helix-coil transition theory fits the data for thermal unfolding transitions of Biopolymers, Vol.

31, ?doi=&rep=rep1&type=pdf.

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