Publication Date:
1984-01-20
Description:
Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Apolipoprotein A-I
;
Apolipoproteins
;
Binding Sites
;
Calcitonin
;
Chemical Phenomena
;
Chemistry
;
Corticotropin-Releasing Hormone
;
Endorphins
;
Glucagon
;
Growth Hormone-Releasing Hormone
;
*Hormones/pharmacology
;
Lipoproteins, HDL
;
Melitten
;
Models, Structural
;
*Peptides/chemical synthesis/metabolism/pharmacology
;
Protein Conformation
;
Structure-Activity Relationship
;
beta-Endorphin
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
