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Literature DB >> 4577793

Proposed tertiary structure for the hypothalamic thyrotropin-releasing factor.

Abstract

Semiempirical energy calculations were performed to determine the conformation of the thyrotropin-releasing factor, L-pyroglutamyl-L-histidyl-L-prolineamide. Our results strongly suggest a "hairpin turn" conformation stabilized by two specific hydrogen bonds. Experimental support for this structure was obtained from proton magnetic resonance by use of chemical shifts and coupling constants with the implied dihedral angles.

Entities: Chemical

Mesh：

Substances：

Year: 1973 PMID： 4577793 PMCID： PMC433449 DOI： 10.1073/pnas.70.4.1166

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

8 in total

1. Stereochemistry of polypeptide chain configurations.

Authors: G N RAMACHANDRAN; C RAMAKRISHNAN; V SASISEKHARAN
Journal: J Mol Biol Date: 1963-07 Impact factor: 5.469

2. Conformational energies and configurational statistics of copolypeptides containing L-proline.

Authors: P R Schimmel; P J Flory
Journal: J Mol Biol Date: 1968-05-28 Impact factor: 5.469

3. Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide.

Authors: K D Gibson; H A Scheraga
Journal: Proc Natl Acad Sci U S A Date: 1967-08 Impact factor: 11.205

4. Orientation restrictions of the peptide hormone, thyrotropin-releasing factor, due to intramolecular hydrogen bonding.

Authors: G Grant; N Ling; J Rivier; W Vale
Journal: Biochemistry Date: 1972-08-01 Impact factor: 3.162

1 in total

1. 13C-nuclear magnetic resonance study of [85% 13C-enriched proline]thyrotropin releasing factor: 13C-13C vicinal coupling constants and conformation of the proline residue.

Authors: W Haar; S Fermandjian; J Vicar; K Blaha; P Fromageot
Journal: Proc Natl Acad Sci U S A Date: 1975-12 Impact factor: 11.205

1 in total

Proposed tertiary structure for the hypothalamic thyrotropin-releasing factor.

1. Stereochemistry of polypeptide chain configurations.

2. Conformational energies and configurational statistics of copolypeptides containing L-proline.

3. Minimization of polypeptide energy. I. Preliminary structures of bovine pancreatic ribonuclease S-peptide.

4. Orientation restrictions of the peptide hormone, thyrotropin-releasing factor, due to intramolecular hydrogen bonding.

Review 5. The hypothalamic hypophysiotropic thyrotropin-releasing factor.

6. Structure of porcine thyrotropin releasing hormone.

7. Characterization of ovine hypothalamic hypophysiotropic TSH-releasing factor.

8. Computation of the sterically allowed conformations of peptides.

1. 13C-nuclear magnetic resonance study of [85% 13C-enriched proline]thyrotropin releasing factor: 13C-13C vicinal coupling constants and conformation of the proline residue.