Preferred conformational state of the N‐terminus section of a bovine growth hormone fragment (residues 96‐133) in water is an omega loop

No abstract is available for this paper.

• Publication year

  1988

• Venue

  Proteins: Structure, Function, and Bioinformatics

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/prot.340040107PMID 3186691
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Location of an alpha-helix in fragment 96-133 from bovine somatotropin by 1H NMR spectroscopy.

  1988cited by this paper
• Determination of local conformational stability in fragment 96-133 of bovine growth hormone by high-resolution H NMR spectroscopy.

  1988cited by this paper
• Helical formation in isolated fragments of bovine growth hormone.

  1987cited by this paper
• Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin.

  1986cited by this paper
• Compact units in proteins.

  1986cited by this paper
• Structural features of prolactins and growth hormones that can be related to their biological properties.

  1986cited by this paper
• Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat.

  1986cited by this paper
• Seeding protein folding

  1986cited by this paper
• Loops in globular proteins: a novel category of secondary structure.

  1986cited by this paper
• Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.

  1985cited by this paper
• An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution.

  1985cited by this paper
• Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm.

  1985cited by this paper
• Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics.

  1985cited by this paper
• Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances.

  1984cited by this paper
• A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular1H−1H proximities in solution

  1984cited by this paper
• Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.

  1983cited by this paper
• Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.

  1983cited by this paper
• Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation

  1981cited by this paper
• Conformation studies of biologically active fragments of bovine growth hormone.

  1977cited by this paper
• Two‐dimensional spectroscopy. Application to nuclear magnetic resonance

  1976cited by this paper
• Peptides of a biologically active tryptic digest of bovine growth hormone.

  1970cited by this paper
• CHEMICAL AND BIOLOGICAL CHARACTERIZATION OF CLINICALLY ACTIVE TRYPTIC DIGESTS OF BOVINE GROWTH HORMONE *

  1968cited by this paper

• Conformational analysis of cyclo(2,9)-Ac-QCRSVEGSCG-OH from the C-terminal loop of human growth hormone.

  2009cites this paper
• Hydrogen bonding, hydrophobicity, packing, and protein folding.

  1993cites this paper
• Antigenic structure of bovine growth hormone: location of a growth enhancing region.

  1991cites this paper
• Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis.

  1989cites this paper