The optical anisotropy of wormlike chains.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1289, doi. 10.1002/bip.360301313
- By:
- Publication type:
- Article
Works matching IS 00063525 AND DT 1990 AND VI 30 AND IP 13/14
Results: 14
1
2
The reliability of wormlike polysaccharide chain dimensions estimated from electron micrographs.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1161, doi. 10.1002/bip.360301303
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- Publication type:
- Article
3
Quantitative IR spectrophotometry of peptide compounds in water (H<sub>2</sub>O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β-, and random coil conformations.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1259, doi. 10.1002/bip.360301310
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- Publication type:
- Article
4
A fourier transform IR study of the gelation of amylose and amylopectin.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1183, doi. 10.1002/bip.360301304
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- Publication type:
- Article
5
A numerical counterion condensation analysis of the B-Z transition of DNA.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1205, doi. 10.1002/bip.360301306
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- Publication type:
- Article
6
The effects of ligands on the conformation of phosphoglycerate kinase: Fluorescence anisotropy decay and theoretical interpretation.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1151, doi. 10.1002/bip.360301302
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- Publication type:
- Article
7
On the kinetics of oligomer binding.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1215, doi. 10.1002/bip.360301307
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- Publication type:
- Article
8
Quantitative IR spectrophotometry of peptide compounds in water (H<sub>2</sub>O) solutions. I. Spectral parameters of amino acid residue absorption bands.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1243, doi. 10.1002/bip.360301309
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- Publication type:
- Article
9
Approach to the limit of counterion condensation.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1191, doi. 10.1002/bip.360301305
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- Publication type:
- Article
10
Quantitative IR spectrophotometry of peptide compounds in water (H<sub>2</sub>O) solutions. III. Estimation of the protein secondary structure.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1273, doi. 10.1002/bip.360301311
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- Publication type:
- Article
11
α-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of αα-tropomyosin.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1231, doi. 10.1002/bip.360301308
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- Publication type:
- Article
12
<sup>1</sup>H-nmr assignments and conformational studies of melanin concentrating hormone in water using two-dimensional nmr.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1291, doi. 10.1002/bip.360301314
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- Publication type:
- Article
13
Masthead.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. fmi, doi. 10.1002/bip.360301301
- Publication type:
- Article
14
The molecular dimensions of G-actin in solution as studied by dynamic light scattering.
- Published in:
- Biopolymers, 1990, v. 30, n. 13/14, p. 1281, doi. 10.1002/bip.360301312
- By:
- Publication type:
- Article