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S. Rao, W. Miller (1973)
Effect of residual side chain blocking groups and side chain charge on polypeptide conformation in aqueous solutionBiopolymers, 12
D. Brant (1968)
Conformational Energy Estimates for Helical Polypeptide MoleculesMacromolecules, 1
P. Flory, W. Leonard (1965)
Thermodynamic Properties of Solutions of Helical PolypeptidesJournal of the American Chemical Society, 87
W. Miller, C. Goebel (1968)
Dimensions of protein random coils.Biochemistry, 7 11
A. Tobolsky (1964)
Isolated Helical MacromoleculesThe Journal of Physical Chemistry, 68
W. Hiltner, A. Hopfinger, A. Walton (1972)
Helix-coil controversy for polyamino acids.Journal of the American Chemical Society, 94 12
D. Aebersold, E. Pysh (1970)
Optical properties of amorphous polypeptides. I. One state solutions.The Journal of chemical physics, 53 6
R. Hawkins, A. Holtzer (1972)
Some Macromolecular Properties of Poly(α-L-glutamic acid) Random CoilsMacromolecules, 5
J. Edsall, P. Flory, J. Kendrew, A. Liquori, G. Némethy, G. Ramachandran, H. Scheraga (1966)
A proposal of standard conventions and nomenclature for the description of polypeptide conformation.The Journal of biological chemistry, 241 4
M. Huggins (1943)
The Structure of Fibrous Proteins.Chemical Reviews, 32
A. Takahashi, M. Nagasawa (1964)
Excluded Volume of Polyelectrolyte in Salt SolutionsJournal of the American Chemical Society, 86
B. Zimm, J. Bragg (1959)
Theory of the Phase Transition between Helix and Random Coil in Polypeptide ChainsJournal of Chemical Physics, 31
J. Rai, W. Miller (1972)
Vapor Sorption of N,N-Dimethylformamide on Poly(γ-benzyl α,L-glutamate)Macromolecules, 5
R. Scott, H. Scheraga (1966)
Conformational Analysis of Macromolecules. III. Helical Structures of Polyglycine and Poly‐L‐AlanineJournal of Chemical Physics, 45
U. Strauss, Edward Smith, P. Wineman (1953)
Polyphosphates as Polyelectrolytes. I. Light Scattering and Viscosity of Sodium Polyphosphates in Electrolyte Solutions1Journal of the American Chemical Society, 75
Yoshihisa Hayashi, A. Teŕamoto, K. Kawahara, H. Fujita (1969)
Solution properties of synthetic polypeptides. V. Helix–coil transition in poly(β‐benzyl L‐aspartate)Biopolymers, 8
J. Edsall, P. Flory, J. Kendrew, A. Liquori, G. Némethy, G. Ramachandran, H. Seheraga (1966)
A proposal of standard conventions and nomenclature for the description of polypeptide conformations: COMMUNICATION TO THE EDITORSBiopolymers, 4
M. Tiffany, S. Krimm (1968)
New chain conformations of poly(glutamic acid) and polylysine.Biopolymers, 6 9
P. Santis, E. Giglio, A. Liquori, A. Ripamonti (1965)
Van Der Waals Interaction and the Stability of Helical Polypeptide ChainsNature, 206
S. Krimm, J. Mark (1968)
Conformations of polypeptides with ionized side chains of equal length.Proceedings of the National Academy of Sciences of the United States of America, 60 4
N. Ise, T. Okubo (1969)
Studies on Aqueous Solutions of Sodium Poly-L-glutamates. Determinations of Mean Activity Coefficients, Osmotic Coefficient, Transference Number, and Partial Molal VolumeMacromolecules, 2
G. Ramachandran, C. Venkatachalam, S. Krimm (1966)
Stereochemical criteria for polypeptide and protein chain conformations. 3. Helical and hydrogen-bonded polypeptide chains.Biophysical journal, 6 6
Robert Snipp, W. Miller, R. Nylund (1965)
The Charge-Induced Helix-Random Coil Transition in Aqueous Solution1Journal of the American Chemical Society, 87
U. Strauss, Edward Smith (1953)
Polyphosphates as Polyelectrolytes. II. Viscosity of Aqueous Solutions of Graham's Salts1Journal of the American Chemical Society, 75
S. Krimm, J. Mark, M. Tiffany (1969)
Influence of counterions on the helical conformations of charged polypeptide chainsBiopolymers, 8
Z. Alexandrowicz (1971)
Intrinsic viscosity of polyelectrolytesThe Journal of Physical Chemistry, 75
G. Némethy, S. Leach, H. Scheraga (1966)
The Influence of Amino Acid Side Chains on the Free Energy of Helix-Coil Transitions1The Journal of Physical Chemistry, 70
E. Bradbury, A. Downie, A. Elliott, W. Hanby (1960)
The stability and screw sense of the α-helix in poly-β-benzyl-L-aspartateProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 259
T. Ooi, R. Scott, G. Vanderkooi, H. Scheraga (1967)
Conformational Analysis of Macromolecules. IV. Helical Structures of Poly‐L‐Alanine, Poly‐L‐Valine, Poly‐β‐Methyl‐L‐Aspartate, Poly‐γ‐Methyl‐L‐Glutamate, and Poly‐L‐TyrosineJournal of Chemical Physics, 46
D. Brant, W. Miller, P. Flory (1967)
Conformational energy estimates for statistically coiling polypeptide chainsJournal of Molecular Biology, 23
S. Lifson (1958)
Neighbor Interactions and Internal Rotations in Polymer Molecules. II. PolyelectrolytesJournal of Chemical Physics, 29
Ptitsyn Ob, Skvortsov Am (1965)
[Theory of helix-coil transformation in biopolymers. V. A method of determining cooperativeness of helix-coil transformation in polypeptide chains by changing molecule size in the transformation region].Biofizika, 10
Seiji Tanaka, A. Nakajima (1970)
Conformational Aspects of Polypeptides Containing lonizable Side ChainsPolymer Journal, 1
Conformational energy estimates were made for completely charged polyglutamic acid with different assumptions concerning the placement of side chain charge. Viewed as a helix, the minimum energy structure is somewhat affected by the side‐chain charge placement. The average energy of the chain viewed as a random coil is equal to or less than the average energy of the chain viewed as a helix. Unlike the polyacrylate chain, nearest‐neighbor charge interaction is shown to increase the chain dimensions. Although the calculations are approximate there is little evidence to suggest that isolated polyglutamate molecules in the absence of added electrolyte should behave as rods or that there are significant amounts of locally ordered structures. Presently no experimental results exist under conditions appropriate to isolated molecular calculations.
Biopolymers – Wiley
Published: Apr 1, 1973
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