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155904-35-1

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155904-35-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 155904-35-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,5,5,9,0 and 4 respectively; the second part has 2 digits, 3 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 155904-35:
(8*1)+(7*5)+(6*5)+(5*9)+(4*0)+(3*4)+(2*3)+(1*5)=141
141 % 10 = 1
So 155904-35-1 is a valid CAS Registry Number.

155904-35-1Relevant articles and documents

Design strategies for the sequence-based mimicry of side-chain display in protein β-sheets by α/β-peptides

Lengyel, George A.,Horne, W. Seth

supporting information, p. 15906 - 15913,8 (2020/08/24)

The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1→1 α→β-residue substitutions at cross-strand positions in a hairpin-forming α-peptide sequence can generate an α/β-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single β-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of αα dipeptide segments for the ability to retain both sheet folding encoded by a parent α-peptide sequence as well as nativelike side-chain display in the vicinity of the β-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.

Use of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide mimics in SH2 antagonists

Davidson,Martin

, p. 9459 - 9464 (2007/10/03)

Novel conformationally constrained phosphotyrosine pseudopeptide derivatives of the tetrapeptide pY-E-E-I were prepared and evaluated as SH2 binding antagonists. (C) 2000 Elsevier Science Ltd.

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