Publication Date:
1995-11-10
Description:
The de novo design of peptides and proteins has recently emerged as an approach for investigating protein structure and function. Designed, helical peptides provide model systems for dissecting and quantifying the multiple interactions that stabilize secondary structure formation. De novo design is also useful for exploring the features that specify the stoichiometry and stability of alpha-helical coiled coils and for defining the requirements for folding into structures that resemble native, functional proteins. The design process often occurs in a series of discrete steps. Such steps reflect the hierarchy of forces required for stabilizing tertiary structures, beginning with hydrophobic forces and adding more specific interactions as required to achieve a unique, functional protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bryson, J W -- Betz, S F -- Lu, H S -- Suich, D J -- Zhou, H X -- O'Neil, K T -- DeGrado, W F -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):935-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉DuPont Merck Pharmaceutical Company, Wilmington, DE 19880, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481798" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Crystallography, X-Ray
;
DNA-Binding Proteins/chemistry
;
Hydrogen Bonding
;
Models, Molecular
;
Molecular Sequence Data
;
*Protein Conformation
;
*Protein Engineering
;
Protein Folding
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Thermodynamics
;
Zinc Fingers
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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