J. Brahms | Semantic Scholar

Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism.

S. Brahms, J. Brahms
Chemistry, Biology
Journal of molecular biology
5 April 1980

Adenylate oligomers in single- and double-strand conformation.

J. Brahms, A. Michelson, K. V. van Holde
Chemistry
Journal of molecular biology
1 February 1966

Identification of β,β-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism

S. Brahms, J. Brahms, G. Spach, A. Brack
Biology, Materials Science
1 August 1977

The similarity in shape between the theoretical curve and the observed CD spectra suggests a dominance of β-turn segments in the poly(Ala2-Gly2) structure, which is also in agreement with the characterization of this polypeptide by solid state methods.

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A STUDY OF CONFORMATION OF NUCLEIC ACIDS IN SOLUTION BY MEANS OF CIRCULAR DICHROISM.

J. Brahms, W. Mommaerts
Biology
Journal of molecular biology
1 October 1964

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Conformational stability of dinucleotides in solution.

J. Brahms, J. Maurizot, A. Michelson
Chemistry
Journal of molecular biology
14 May 1967

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Effect of non-histone proteins on thermal transition of chromatin and of DNA.

N. Defer, A. Kitzis, J. Kruh, S. Brahms, J. Brahms
Biology
Nucleic acids research
1 July 1977

It is concluded that chromatin non-histone proteins contain different fractions of proteins which are causing stabilizing and destabilizing effect on DNA structure.

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Form of DNA and the nature of interactions with proteins in chromatin.

D. C. Goodwin, J. Brahms
Chemistry, Biology
Nucleic acids research
1 March 1978

For the first time, chromatins of different origins with increasing content of non-histone proteins have been investigated by Raman spectroscopy and it is proposed that the mechanism of specific recognition in chromatin involves the large groove.

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Direct evidence of the C-like form of sodium deoxyribonucleate.

J. Brahms, J. Pilet, T. T. Phuong Lan, L. R. Hill
Biology
Proceedings of the National Academy of Sciences…
1 December 1973

From infrared linear dichroism studies, direct evidence is given for a new Na DNA form, which is similar to the C form of Li DNA, which may be biologically important and have a possible role for recognition by proteins.

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Activation and inhibition of transcription by supercoiling.

J. Brahms, O. Dargouge, S. Brahms, Y. Ohara, V. Vagner
Biology
Journal of molecular biology
20 February 1985

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Structural investigations on DNA·protamine complexes

T. T. Herskovits, J. Brahms
Chemistry, Biology
Biopolymers
1 April 1976

A model of the protamine·DNA complex is proposed, which suggests that the presence of apolar amino‐acid residues, and probably the folding of the polypeptide chain, is responsible for preventing the B‐to‐A transition.

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