Beta Turn Conformation
Beta Turn Conformation is a type of secondary structure in proteins characterized by a tight reversal of the polypeptide chain involving four amino acid residues, where the carbonyl group of the first residue forms a hydrogen bond with the amino group of the fourth residue, stabilizing a bend in the backbone.
592
Publications
34.4K
Citations
2.1K
Authors
573
Institutions
Publications per year
2017–2026
16
Variants
Beta-turn Conformation
Parents
592
1–5 of 592
2.1K
18
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United States Naval Research Laboratory, United States
12 publications · 657 citations
12
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1–5 of 2.1K
573

Indian Institute of Science Bangalore
Bengaluru, India
28 h-index
127 publications
5.7K citations

University of Padua
Padua, Italy
17 h-index
81 publications
3K citations

Centre National de la Recherche Scientifique
Paris, France
16 h-index
115 publications
3.8K citations

Eötvös Loránd University
Budapest, Hungary
12 h-index
24 publications
833 citations

Cornell University
Ithaca, United States
10 h-index
19 publications
1.5K citations
Université de Montréal
Montreal, Canada
10 h-index
31 publications
1.8K citations

Brandeis University
Waltham, United States
9 h-index
16 publications
1.2K citations
Scripps Research Institute
San Diego, United States
9 h-index
28 publications
5.2K citations
1–8 of 573
JACS · 46 publications · 3.7K citations
35
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58 publications · 2.2K citations
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JMB · 25 publications · 2.9K citations
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JOC · 25 publications · 775 citations
21
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PNAS · 22 publications · 3.2K citations
20
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