Literature DB >> 5233472

Nuclear magnetic resonance studies of proteins. I. Conformational variance among members of the chymotrypsinogen family.

D P Hollis, G McDonald, R L Biltonen.   

Abstract

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Year:  1967        PMID： 5233472      PMCID： PMC335698          DOI： 10.1073/pnas.58.2.758

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


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  6 in total

1.  THE EFFECT OF TEMPERATURE ON THE PROTON MAGNETIC RESONANCE SPECTRA OF RIBONUCLEASE, OXIDIZED RIBONUCLEASE, AND LYSOZYME.

Authors:  M MANDEL
Journal:  Proc Natl Acad Sci U S A       Date:  1964-09       Impact factor: 11.205

2.  PREFERENTIAL OXIDATION OF THE METHIONINE RESIDUE NEAR THE ACTIVE SITE OF CHYMOTRYPSIN.

Authors:  H SCHACHTER; G H DIXON
Journal:  J Biol Chem       Date:  1964-03       Impact factor: 5.157

3.  PROTON MAGNETIC RESONANCE SPECTRA OF SOME PROTEINS. I. RIBONUCLEASE, OXIDIZED RIBONUCLEASE, LYSOZYME, AND CYTOCHROME C.

Authors:  M MANDEL
Journal:  J Biol Chem       Date:  1965-04       Impact factor: 5.157

4.  Nuclear magnetic resonance studies of proteins.

Authors:  A KOWALSKY
Journal:  J Biol Chem       Date:  1962-06       Impact factor: 5.157

5.  Proton magnetic resonance spectra of amino acids.

Authors:  O JARDETZKY; C D JARDETZKY
Journal:  J Biol Chem       Date:  1958-08       Impact factor: 5.157

6.  Validity of the "two-state" hypothesis for conformational transitions of proteins.

Authors:  R Lumry; R Biltonen
Journal:  Biopolymers       Date:  1966-09       Impact factor: 2.505
  6 in total

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