ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Protein Conformation
  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (6)
  • San Francisco, CA
  • 1975-1979  (6)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (6)
  • San Francisco, CA
  • Wiley-Blackwell  (1,712)
Years
Year
  • 1
    facet.materialart.
    Unknown
    A structural model for the kinetic behavior of hemoglobin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-11-30
    Description: The tertiary structures of all liganded hemoglobins in the R state differ in detail. Steric hindrance arising from nonbonded ligand-globin interactions affects the binding of ligands such as CO and cyanide which preferentially form linear axial complexes to heme; these ligands bind in a strained off-axis configuration. Ligands such as O2 and NO, which preferentially form bent complexes, encounter less steric hindrance and can bind in their (preferred) unstrained configuration. Linear complexes distort the ligand pockets in the R state (and by inference, in the T state) more than bent complexes. These structural differences between linear and bent complexes are reflected in the kinetic behavior of hemoglobin. Structural interpretation of this kinetic behavior indicates that the relative contributions of nonbonded ligand-globin interactions and nonbonded heme interactions to transition state free energies differ for linear and bent ligands. The relative contributions of these interactions to the free energy of cooperativity may also differ for linear and bent ligands. Thus the detailed molecular mechanism by which the affinity of heme is regulated differs for different ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, K -- Deatherage, J F -- Seybert, D W -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1035-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493990" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Heme/*metabolism ; Hemoglobins/metabolism ; Horses ; Kinetics ; Ligands ; Oxygen/*metabolism ; Oxyhemoglobins/*metabolism ; Protein Conformation ; Stereoisomerism ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Structure of collagen in cartilage of intervertebral disk (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-02-03
    Description: Small-angle x-ray and neutron diffraction patterns have been obtained from the annulus fibrosus of porcine intervertebral disk. These show that the collagen in this tissue is modified compared with that in tendon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berthet, C -- Hulmes, D J -- Miller, A -- Timmins, P A -- New York, N.Y. -- Science. 1978 Feb 3;199(4328):547-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/622556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Collagen ; Glycosaminoglycans ; Intervertebral Disc/*ultrastructure ; Neutrons ; Protein Conformation ; Proteoglycans ; Scattering, Radiation ; Swine ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Channel structures of gramicidin: characterization of succinyl derivatives (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-28
    Description: Succinyl derivatives of gramicidin were tested for their ability to form channels in planar artificial lipid bilayers. Both N-succinyldeformylgramicidin methyl ester and charged O-succinylgramicidin formed channels, but the channels had markedly different sizes and lifetimes. This implies that gramicidin forms channels by end-to-end association. However, the doubly charged N,O-bissuccinyldeformylgramicidin was inactive, which suggests that only end-to-end association of gramicidin may result in channel formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradley, R J -- Urry, D W -- Okamoto, K -- Rapaka, R -- New York, N.Y. -- Science. 1978 Apr 28;200(4340):435-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/77040" target="_blank"〉PubMed〈/a〉
    Keywords: Electric Conductivity ; *Gramicidin ; Hydrogen Bonding ; Ionophores ; Membranes, Artificial ; Protein Conformation ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Conformation of [Leu5]enkephalin from X-ray diffraction: features important for recognition at opiate receptor (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-17
    Description: The conformation of [Leu5]enkephalin is produced by a Tyr-Gly-Gly-Phe beta bend stabilized by antiparallel hydrogen bonding between tyrosine and phenylalanine. On the basis of a comparison of the observed structure with the structure of known opiate agonists, three hydrophilic and two hydrophobic regions have been identified as contributing to the recognition of the molecule at the opiate receptor site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, D -- Griffin, J F -- New York, N.Y. -- Science. 1978 Mar 17;199(4334):1214-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/204006" target="_blank"〉PubMed〈/a〉
    Keywords: *Endorphins/metabolism ; *Enkephalins/metabolism ; Hydrogen Bonding ; Models, Molecular ; Morphine ; Protein Conformation ; Receptors, Opioid/metabolism ; Structure-Activity Relationship ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Crystal structure of [Leu5]enkephalin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blundell, T L -- Hearn, L -- Tickle, I J -- Palmer, R A -- Morgan, B A -- Smith, G D -- Griffin, J F -- New York, N.Y. -- Science. 1979 Jul 13;205(4402):220.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451597" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; *Endorphins ; *Enkephalins ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    Acridine araphanes: a new class of probe molecules for biological systems (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-21
    Description: The bis-acridine ring system forms the basis for new biophysical probes of novel stereochemistry. Spectral data indicate that certain alkylene bridged bis-9-aminoacridines have a parallel plane conformation of predictable interplane distance. The parallel plane conformation is independent of solvent and thus is different from nucleic acid systems. This stable conformation allows these compounds to be used as sensitive "rulers" for describing binding site geometry in cholinergic enzymes and in the delineation of the mechanism of allosteric control in acetylcholinesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Himel, C M -- Taylor, J L -- Pape, C -- Millar, D B -- Christopher, J -- Kurlansik, L -- New York, N.Y. -- Science. 1979 Sep 21;205(4412):1277-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472743" target="_blank"〉PubMed〈/a〉
    Keywords: *Acetylcholinesterase/metabolism ; *Acridines ; Binding Sites ; Kinetics ; Molecular Conformation ; Phosphorylation ; Protein Conformation ; Spectrophotometry, Ultraviolet
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...