Results 241 to 250 of about 4,667,155 (305)

Peptide Mimetic Platform for Activity Profiling of Mycobacterial l,d-Transpeptidases. [PDF]

Biochemistry
Ocius KL, Sanborn RE, Naick A, Brammer Basta LA, Pires MM.   +4 more
europepmc   +1 more source

The Synergy of Macrocycles and Heterocycles: A Review of Coordination Behavior, Sensing, and Functional Materials Based on Calixarenes. [PDF]

Molecules
Kalinin V, Padnya P, Stoikov I.
europepmc   +1 more source

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A Novel Cross-Linking Reagent for Bovine Hemoglobin Modification

Biotechnology Letters, 2003
A novel cross-linking reagent, methoxypolyethelene glycol-glutamic acid, was synthesized and used to modify bovine hemoglobin. Bis-tetrameric hemoglobin with moderate affinity for O2 was obtained under the controlled reaction conditions.
Xiuling Lu, Zhiguo Su
exaly   +3 more sources

Chemical Cross-Linking: Reagents and Problems in Studies of Membrane Structure

Annual Review of Biochemistry, 1977
INTRODUCTION AND PERSPECTIVE ....... 524 THE PROCEDURE AND THE PROBLEMS. . . . . .... ...... . . .. . ... . . .... .... . 525 CHEMISTRY OF SELECTED REAGENTS 527 Alkyl Imidates (lmidoesters} 527 Synthesis 528 Reaction paths and mechanisms 528 Use as modifYing reagents 531 Acyl Azides 532 Sulfhydryl Reagents 532 Nitrenes 534 ...
K, Peters, F M, Richards
exaly   +3 more sources

Bifunctional imidoesters as cross-linking reagents

Biochemical and Biophysical Research Communications, 1966
Abstract Bifunctional small molecule reagents have been important in the study of a number of problems in protein chemistry (cf. Wold, 1961 a, b; Zahn and Meienhofer, 1958 ; Singer, 1959 ). For most purposes it is desirable that the chemical modifications produced by the bifunctional reagent cause as little alteration as possible in the conformation
A, Dutton, M, Adams, S J, Singer
openaire   +2 more sources

Synthesis of “long,” hydrophilic, protein-cross-linking reagents

Analytical Biochemistry, 1974
Abstract Since most of the protein cross-linking reagents in use are strongly hydrophobic, their length cannot be increased beyond approximately 20 A between the protein-reactive groups, before denaturation of most proteins becomes noticeable at already a very few cross-links per molecule.
K, Wetz, H, Fasold, C, Meyer
openaire   +2 more sources