Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Sequential assignment and secondary structure

Biochemistry ◽  
1993 ◽  
Vol 32 (42) ◽  
pp. 11345-11351 ◽  
Author(s):  
Corinne Cerf ◽  
Guy Lippens ◽  
Serge Muyldermans ◽  
Alain Segers ◽  
V. Ramakrishnan ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Histone H1 ◽  
Sequential Assignment ◽  
Globular Domain ◽  
Two Dimensional ◽  
Nmr Studies

Homo- and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Full Assignment, Tertiary Structure, and Comparison with the Globular Domain of Histone H5

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11079-11086 ◽  
Author(s):  
Corinne Cerf ◽  
Guy Lippens ◽  
V. Ramakrishnan ◽  
Serge Muyldermans ◽  
Alain Segers ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Histone H1 ◽  
Globular Domain ◽  
Two Dimensional ◽  
Nmr Studies ◽  
Histone H5

scholarly journals The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

1990 ◽  
Vol 265 (3) ◽  
pp. 739-746 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
I De Baere ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Secondary Structure ◽  
Alpha Helix ◽  
Histone H1 ◽  
Globular Domain ◽  
Nematode Caenorhabditis Elegans ◽  
Terminal Domain ◽  
Helix Formation ◽  
A Minor

The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.

Two-dimensional proton NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure

Biochemistry ◽  
1991 ◽  
Vol 30 (46) ◽  
pp. 11186-11192 ◽  
Author(s):  
Hans Robert Kalbitzer ◽  
Klaus Peter Neidig ◽  
Wolfgang Hengstenberg
Keyword(s):  
Staphylococcus Aureus ◽  
Secondary Structure ◽  
Proton Nmr ◽  
Two Dimensional ◽  
Nmr Studies

scholarly journals Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution

1990 ◽  
Vol 193 (3) ◽  
pp. 789-795 ◽  
Author(s):  
Chin YU ◽  
Chang-Shin LEE ◽  
Li-Chin CHUANG ◽  
You-Rhon SHEI ◽  
Chi Ying WANG
Keyword(s):  
Aqueous Solution ◽  
Secondary Structure ◽  
Two Dimensional ◽  
Nmr Studies

Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin. Resonance assignments and secondary structure

1991 ◽  
Vol 199 (2) ◽  
pp. 285-291 ◽  
Author(s):  
David SIPOS ◽  
Kasibhatla CHANDRASEKHAR ◽  
Klas ARVIDSSON ◽  
Ake ENGSTROM ◽  
Anders EHRENBERG
Keyword(s):  
Secondary Structure ◽  
Proton Nmr ◽  
Resonance Assignments ◽  
Two Dimensional ◽  
Hybrid Peptide ◽  
Nmr Studies ◽  
Cecropin A
Sign in / Sign up

Export Citation Format

Share Document